[ccp4bb] NSLS II & CFN User Meeting - LAST DAY submission ABSTRACTS - May 13 - X-ray based technologies in emerging fuel cell research

[Stojanoff, Vivian]

LAST DAY to SUBMIT ABSTRACTS for POSTERS

Dear Colleagues


We are pleased to announce the workshop entitled "X-ray based technologies in 
emerging fuel cell research " scheduled during the NSLS II and CFN User Meeting 
(Workshop 3 
Agenda.docx),
 this coming May 13, programed for in-person participation. Researchers working 
in photosynthesis and redox enzymes are encouraged to apply as several talks 
are focused on them.

To REGISTER for visit: 
https://www.bnl.gov/usersmeeting/index.php



Participants, including students and postdocs, are encouraged to present their 
results in the poster session.  Limited funds are available  to sponsor  
participants especially at graduate or post-doctoral levels for this one day 
workshop. To apply for funding please complete the form:


https://forms.gle/A8doqMJXxVoEAJED6



VENUE:

This one day workshop  aims to bring together researchers, beamline scientists, 
and developers, who seek to advance our knowledge on fuel cells  towards 
sustainable energy models. The goal is to discuss recent advances and the 
current status of the various techniques used to characterize natural and 
artificial model systems including their limitations (both x-ray as well as 
non-x-ray techniques). The expectation is that participants will find an 
environment in which discussions allow the collaborations among researchers and 
those responsible for the increased understanding of new systems through the 
development of new techniques.



Confirmed  SPEAKERS:

Kara Bren (Univ Rochester), Todd Deutsch (NREL), Petra Fromme (ASU), Masakazu 
Iwai (LBL), Mathias Kling (LCLS), Yi Lu ( Univ Texas), Smaranda Marinescu 
(USC), Sean McSweeney (NSLS II), Jose Henrique Pereira (JBEI), Gabriela 
Schlau-Cohen (MIT), Narayanasami Sukumar (Cornel University), Francesca Maria 
Toma (Heoron Institute, Germany).


For further questions please contact the organizers:


Dr. Vivian Stojanoff   |Dr. N. Sukumar

Education, Training, Outreach |Sector 24, Cornell University

User Program |Building 436E, APS

Center of Biomolecular Structure   |   Argonne National Laboratory

NSLS II, Building 745  |   9700, S. Cass Ave

Brookhaven National Laboratory|   Argonne, IL 60439

Upton NY 11973 |   e-mail: 
suku...@anl.gov

e-mail: stoja...@bnl.gov>   |   Tel: 
630-252-0681

phone: 631-344-8375





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[ccp4bb] Invitation to participate in person NSLS II & CFN workshop #3

[Stojanoff, Vivian]

Dear Colleagues


You are invited to attend the workshop entitled "X-ray based technologies in 
emerging fuel cell research " scheduled during the NSLS II and CFN User Meeting 
(Workshop 3 
Agenda.docx),
 this coming May 13, 
(https://www.bnl.gov/usersmeeting/index.php)
 programed for in-person participation. Researchers working in photosynthesis 
and redox enzymes are encouraged to apply as several talks are focused on them.

To REGISTER for visit: https://www.bnl.gov/usersmeeting/reg/step1.php  LAST DAY 
TO REGISTER MAY 1st. Registration will reopen May 12



Participants, including students and postdocs, are encouraged to present their 
results in the poster session.  Limited funds are available  to sponsor  
participants especially at graduate or post-doctoral levels for this one day 
workshop. To apply for funding please register and complete the form:


https://forms.gle/A8doqMJXxVoEAJED6



VENUE:

This one day workshop  aims to bring together researchers, beamline scientists, 
and developers, who seek to advance our knowledge on fuel cells  towards 
sustainable energy models. The goal is to discuss recent advances and the 
current status of the various techniques used to characterize natural and 
artificial model systems including their limitations (both x-ray as well as 
non-x-ray techniques). The expectation is that participants will find an 
environment in which discussions allow the collaborations among researchers and 
those responsible for the increased understanding of new systems through the 
development of new techniques.



Confirmed  SPEAKERS:

Kara Bren (Univ Rochester), Todd Deutsch (NREL), Petra Fromme (ASU), Masakazu 
Iwai (LBL), Mathias Kling (LCLS), Yi Lu ( Univ Texas), Smaranda Marinescu 
(USC), Sean McSweeney (NSLS II), Jose Henrique Pereira (JBEI), Gabriela 
Schlau-Cohen (MIT), Narayanasami Sukumar (Cornel University), Francesca Maria 
Toma (Heoron Institute, Germany).


For further questions please contact the organizers:


Dr. Vivian Stojanoff   |Dr. N. Sukumar

Education, Training, Outreach |Sector 24, Cornell University

User Program |Building 436E, APS

Center of Biomolecular Structure   |   Argonne National Laboratory

NSLS II, Building 745  |   9700, S. Cass Ave

Brookhaven National Laboratory|   Argonne, IL 60439

Upton NY 11973 |   e-mail: 
suku...@anl.gov

e-mail: stoja...@bnl.gov>   |   Tel: 
630-252-0681

phone: 631-344-8375






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[ccp4bb] CBMS Structural Biology Workbench - June 3 to 6, 2024

[Stojanoff, Vivian]

Dear All, Share with new members in your group

You are cordially invited to join the CBMS Structural Biology Workbench, June 3 
to 6. All practical sessions will be held in-person. To participate  in-person, 
participants need to register for the workbench and have an active BNL Guest 
Appointment.

To register:  https://www.bnl.gov/cbmsworkbench/index.php   Choose from remote 
or in-person registration. Remote registration is free.

In-person participation is limited and requires an Active Brookhaven Guest 
Appointment.  In-person participation ONLY if you have an active BNL Guest 
Appointment.

CBMS Team




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[ccp4bb] REMINDER >>> CBMS Lecture Series - Narayanasami Sukumar - April 17

[Stojanoff, Vivian]

You are cordially invited to join  the Center for Biomolecular Structure 
Lecture Series ………..





 Narayanasami Sukumar


Cornell University


NE CAT, Advance Photon Source





WEDNESDAY, April 17, 13:30 (EDT)



"An in-depth study on electron transfer mechanism in cupredoxins"



Register in advance for this meeting:


https://bnl.zoomgov.com/meeting/register/vJIsdOyppjIuE9myS_Utu_WtaGoyVnNkXBI



   Time conversion Link: 
https://www.worldtimebuddy.com/


 ABSTRACT: Electron transfer (ET) through and between proteins is a frequently 
occurring biological process in both prokaryotes and eukaryotes. Understanding 
the principle behind the ET will help to understand the important biological 
processes like respiration and photosynthesis. The major focus of the talk 
would be on the type I copper protein, amicyanin which accepts electrons from 
quinone cofactor of methylamine dehydrogenase and donates them to a c-type 
cytochrome over long distance. Along with amicyanin, the talk would cover the 
following: (a) another type I copper protein azurin in complex with 
quinoprotein aromatic amine dehydrogenase, (b) role of dynamics in crystalline 
state, analyzed by joint x-ray and neutron study, (c) mutational studies on 
amicyanin, and (d) charge density/ultra-high-resolution studies on amicyanin 
which are currently in progress. Several instances where synchrotron 
crystallography played important role in elucidating catalytic mechanism will 
be discussed.



==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e lifescie...@bnl.gov

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973





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[ccp4bb] CBMS Structural Biology Workbenches - June 3 to 6

[Stojanoff, Vivian]

Dear Colleagues

You are invited to register for the CBMS Structural Biology Workbench scheduled 
June 3 - 6, at the National Synchrotron Light Source II At Brookhaven National 
Laboratory.  This workbench will be hybrid with practical sessions being in 
person.

LAST DAY TO REGISTER for IN-PERSON PARTICIPATION APRIL 15

Motivation

The CBMS Structural Biology workbench includes Solution Scattering (SAXS/WAXS), 
X-ray Foot Printing (XFP) and Macromolecular Crystallography (MX). The workshop 
spans over four days of virtual and in person training classes aimed at 
researchers that would like to know more about techniques and methods available 
to scientists at BNL's Center for Biomolecular Structure (CBMS) structural 
biology beamlines. The aim of the CBMS workbenches is to provide training to 
members of the community and an opportunity to collect preliminary data to 
support future beamtime proposals within the CBMS Structural Biology beamlines.

In-person attendees are encouraged to bring their own samples. Interested 
participants are invited to register for one or both of the following 
workbenches: Biomolecular Solutions Scattering and Macromolecular 
Crystallography.

Agenda

DRAFT AGENDA Attached.



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CBMS-SB_Workbench-Draft Agenda .xlsx
Description: CBMS-SB_Workbench-Draft Agenda .xlsx

[ccp4bb] CBMS Lecture Series - Narayanasami Sukumar - April 17

[Stojanoff, Vivian]

You are cordially invited to join  the Center for Biomolecular Structure 
Lecture Series ………..





 Narayanasami Sukumar


Cornell University


NE CAT, Advance Photon Source





WEDNESDAY, April 17, 13:30 (EDT)



"An in-depth study on electron transfer mechanism in cupredoxins"



Register in advance for this meeting:


https://bnl.zoomgov.com/meeting/register/vJIsdOyppjIuE9myS_Utu_WtaGoyVnNkXBI



   Time conversion Link: 
https://www.worldtimebuddy.com/




==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e lifescie...@bnl.gov

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973





To unsubscribe from the CCP4BB list, click the following link:
https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB=1

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[ccp4bb] NSLS II & CFN User Meeting - May 13 - X-ray based technologies in emerging fuel cell research

[Stojanoff, Vivian]

Dear Colleagues


We are pleased to announce the workshop entitled "X-ray based technologies in 
emerging fuel cell research " scheduled during the NSLS II and CFN User Meeting 
(Workshop 3 
Agenda.docx),
 this coming May 13, programed for in-person participation. Researchers working 
in photosynthesis and redox enzymes are encouraged to apply as several talks 
are focused on them.

To REGISTER for visit: 
https://www.bnl.gov/usersmeeting/index.php



Participants, including students and postdocs, are encouraged to present their 
results in the poster session.  Limited funds may be available  to sponsor  
participants especially at graduate or post-doctoral levels. To apply for 
funding please complete the form:


https://forms.gle/A8doqMJXxVoEAJED6



VENUE:

This one day workshop  aims to bring together researchers, beamline scientists, 
and developers, who seek to advance our knowledge on fuel cells  towards 
sustainable energy models. The goal is to discuss recent advances and the 
current status of the various techniques used to characterize natural and 
artificial model systems including their limitations (both x-ray as well as 
non-x-ray techniques). The expectation is that participants will find an 
environment in which discussions allow the collaborations among researchers and 
those responsible for the increased understanding of new systems through the 
development of new techniques.



Confirmed  SPEAKERS:

Kara Bren (Univ Rochester), Todd Deutsch (NREL), Petra Fromme (ASU), Masakazu 
Iwai (LBL), Mathias Kling (LCLS), Yi Lu ( Univ Texas), Smaranda Marinescu 
(USC), Sean McSweeney (NSLS II), Jose Henrique Pereira (JBEI), Gabriela 
Schlau-Cohen (MIT), Narayanasami Sukumar (Cornel University), Francesca Maria 
Toma (Heoron Institute, Germany).


For further questions please contact the organizers:


Dr. Vivian Stojanoff   |Dr. N. Sukumar

Education, Training, Outreach |Sector 24, Cornell University

User Program |Building 436E, APS

Center of Biomolecular Structure   |   Argonne National Laboratory

NSLS II, Building 745  |   9700, S. Cass Ave

Brookhaven National Laboratory|   Argonne, IL 60439

Upton NY 11973 |   e-mail: 
suku...@anl.gov

e-mail: stoja...@bnl.gov>   |   Tel: 
630-252-0681

phone: 631-344-8375





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[ccp4bb] Reminder: CBMS Lecture Series; Dessen, March 20.

[Stojanoff, Vivian]

You are cordially invited to join  the Center for Biomolecular Structure 
Lecture Series ………..





Andrea Dessen


CNRS Research Director


Institut de Biologie Structurale, France





WEDNESDAY, March 20, 13:30 (EDT)



"Architecture and Genomic Arrangement of Bacterial Cell Biosynthesis Complexes"



Register in advance for this meeting:


https://bnl.zoomgov.com/meeting/register/vJIsdOysqzoiHJzcKLSKZqX5jfwZQcIozkM



   Time conversion Link: 
https://www.worldtimebuddy.com/



Abstract: The bacterial cell wall is important for survival and shape, and its 
biosynthetic mechanism is the target of beta-lactam antibiotics. The spread of 
resistant strains, however, has limited the usefulness of these drugs and calls 
for efforts towards studies of cell wall formation that could lead to the 
development of innovative treatments. My group is interested in structurally 
and functionally characterizing protein complexes involved in both cytoplasmic 
and periplasmic steps of cell wall biosynthesis. The synthesis of 
peptidoglycan, the main component of the cell wall, starts in the cytoplasm, 
through sequential reactions catalyzed by Mur enzymes that have been suggested 
to associate into a multi-membered complex. This idea is supported by the 
observation that in many bacteria, mur genes are present in a single operon 
within the well conserved dcw cluster, and in some cases pairs of mur genes are 
fused to encode a single, chimeric polypeptide able to catalyze successive 
reactions. I will present the crystal structure of the MurE-MurF chimera from 
Bordetella pertussis, which reveals a head-to-tail, elongated architecture and 
indicates how sequential reactions could be catalyzed. In addition, I will also 
discuss structural details of complexes formed in the bacterial periplasm, 
notably between Penicillin-Binding Proteins (PBPs) and the scaffolding protein 
MreC, that act in partnership with Mur proteins in the cell wall biosynthesis 
process. These structural and functional insights shed light on the importance 
of studying pathways that are of critical relevance for bacterial cell survival 
in light of the antibiotic resistance crisis..



==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e lifescie...@bnl.gov

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973



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[ccp4bb] CBMS Lecture Series - Andrea Dessen - March 20

[Stojanoff, Vivian]

You are cordially invited to join  the Center for Biomolecular Structure 
Lecture Series ………..





Andrea Dessen


CNRS Research Director


Institut de Biologie Structurale, France





WEDNESDAY, March 20, 13:30 (EDT)



"Architecture and Genomic Arrangement of Bacterial Cell Biosynthesis Complexes"



Register in advance for this meeting:


https://bnl.zoomgov.com/meeting/register/vJIsdOysqzoiHJzcKLSKZqX5jfwZQcIozkM



   Time conversion Link: 
https://www.worldtimebuddy.com/



Abstract: The bacterial cell wall is important for survival and shape, and its 
biosynthetic mechanism is the target of beta-lactam antibiotics. The spread of 
resistant strains, however, has limited the usefulness of these drugs and calls 
for efforts towards studies of cell wall formation that could lead to the 
development of innovative treatments. My group is interested in structurally 
and functionally characterizing protein complexes involved in both cytoplasmic 
and periplasmic steps of cell wall biosynthesis. The synthesis of 
peptidoglycan, the main component of the cell wall, starts in the cytoplasm, 
through sequential reactions catalyzed by Mur enzymes that have been suggested 
to associate into a multi-membered complex. This idea is supported by the 
observation that in many bacteria, mur genes are present in a single operon 
within the well conserved dcw cluster, and in some cases pairs of mur genes are 
fused to encode a single, chimeric polypeptide able to catalyze successive 
reactions. I will present the crystal structure of the MurE-MurF chimera from 
Bordetella pertussis, which reveals a head-to-tail, elongated architecture and 
indicates how sequential reactions could be catalyzed. In addition, I will also 
discuss structural details of complexes formed in the bacterial periplasm, 
notably between Penicillin-Binding Proteins (PBPs) and the scaffolding protein 
MreC, that act in partnership with Mur proteins in the cell wall biosynthesis 
process. These structural and functional insights shed light on the importance 
of studying pathways that are of critical relevance for bacterial cell survival 
in light of the antibiotic resistance crisis..



==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e lifescie...@bnl.gov

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973





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[ccp4bb] Reminder: CBMS Lecture Series - Olga Rechkoblit - February 21st, 13:30 (EST)

[Stojanoff, Vivian]

You are cordially invited to join  the Center for Biomolecular Structure 
Lecture Series ………..





Olga  Rechkoblit

Mount Sinai School of Medicine



WEDNESDAY, February 21, 13:30 (EST)



"Activation of bacterial immune system by cyclic nucleotides"



Register in advance for this meeting:


https://bnl.zoomgov.com/meeting/register/vJIsdOGprDojEjg7-CJFcbqdzjJEXsKmbYk



   Time conversion Link: 
https://www.worldtimebuddy.com/



Abstract: The bacterial CBASS system is similar to the cGAS-STING system in 
humans, containing an enzyme that synthesizes a cyclic nucleotide upon viral 
infection and an effector that senses the second messenger for the anti-viral 
response. Cap5, containing a SAVED domain coupled to an HNH DNA endonuclease 
domain, is the most abundant CBASS effector, yet the mechanism by which it 
becomes activated for cell killing remains unknown. We present here 
high-resolution structures of full-length Cap5 from Pseudomonas syringae (Ps) 
with second messengers. The key to PsCap5 activation is a dimer-to-tetramer 
transition, whereby the binding of second messenger to dimer triggers an 
open-to-closed transformation of the SAVED domains, furnishing a surface for 
assembly of the tetramer. This movement propagates to the HNH domains, 
juxtaposing and converting two HNH domains into states for DNA destruction. 
These results show how Cap5 effects bacterial cell suicide and we provide 
proof-in-principle data that the CBASS can be extrinsically activated to limit 
bacterial infections.



==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e lifescie...@bnl.gov

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973





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[ccp4bb] CBMS Lecture Series - Olga Rechkoblit - February 21st, 13:30 (EST)

[Stojanoff, Vivian]

You are cordially invited to join  the Center for Biomolecular Structure 
Lecture Series ………..





Olga  Rechkoblit

Mount Sinai School of Medicine



WEDNESDAY, February 21, 13:30 (EST)



"Activation of bacterial immune system by cyclic nucleotides"



Register in advance for this meeting:


https://bnl.zoomgov.com/meeting/register/vJIsdOGprDojEjg7-CJFcbqdzjJEXsKmbYk



   Time conversion Link: 
https://www.worldtimebuddy.com/



Abstract: The bacterial CBASS system is similar to the cGAS-STING system in 
humans, containing an enzyme that synthesizes a cyclic nucleotide upon viral 
infection and an effector that senses the second messenger for the anti-viral 
response. Cap5, containing a SAVED domain coupled to an HNH DNA endonuclease 
domain, is the most abundant CBASS effector, yet the mechanism by which it 
becomes activated for cell killing remains unknown. We present here 
high-resolution structures of full-length Cap5 from Pseudomonas syringae (Ps) 
with second messengers. The key to PsCap5 activation is a dimer-to-tetramer 
transition, whereby the binding of second messenger to dimer triggers an 
open-to-closed transformation of the SAVED domains, furnishing a surface for 
assembly of the tetramer. This movement propagates to the HNH domains, 
juxtaposing and converting two HNH domains into states for DNA destruction. 
These results show how Cap5 effects bacterial cell suicide and we provide 
proof-in-principle data that the CBASS can be extrinsically activated to limit 
bacterial infections.



==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e lifescie...@bnl.gov

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973





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[ccp4bb] CBMS Structural Biology Workbench - January 29th to February 1st

[Stojanoff, Vivian]

Dear All

You are cordially invited to join the CBMS Structural Biology Workbench talks, 
in specific the Joint Session Lectures. To register:
https://bnl.zoomgov.com/meeting/register/vJIscO2gqzIrG34C30-fi43VRwl0DudNzbw

Monday January 29 at noon (EST)

  Overview of the CBMS Program  - Sean McSweeney (BNL - CBMS) 


  The Bioimaging program at NSLS II - Yong Chu (BNL – NSLS II)

Tuesday January 30 at noon (EST)
  Radiation Damage - Enrique Rudino Pinera (UNAM)

Wednesday Jaunuary 31 at noon (EST)

  Accelerating Drug Discovery: a novel in silico Virtual Screening method 
for SARS- CoV-2 Main Protease -

Xiaogang (Stan) Li (SBU)


Thursday February 1st at noon (EST)

  Synchrotron X-ray Footprinting at 17-BM for Structural Biology - Erik 
Farquhar (Case Western Reserve  University) 


and other lectures offered during the workbench ( 
[https://res.cdn.office.net/assets/mail/file-icon/png/docx_16x16.png] 
CBMS_Workbench_SB-Agenda-29Jan_1Feb_2024_JB.docx)



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e lifescie...@bnl.gov

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973






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[ccp4bb] Reminder: CBMS Lecture Series - Erik Debler

[Stojanoff, Vivian]

You are cordially invited to join  the Center for Biomolecular Structure 
Lecture Series ………..





Erik Debler

Thomas Jefferson University



WEDNESDAY, January 24, 13:30 (EST)



"Hybrid methods to investigate the mechanism of Dot1 histone-modifying enzymes 
in kinetoplastid parasites"



Register in advance for this meeting:



 https://bnl.zoomgov.com/meeting/register/vJItcu2grTotGGdsWXVwtDa4OIkqHcJgvpA



   Time conversion Link: 
https://www.worldtimebuddy.com/



Abstract: Kinetoplastid parasites are medically important eukaryotes that are 
responsible for severe neglected tropical diseases including sleeping sickness 
caused by Trypanosoma brucei. Kinetoplastids have diverged early on in 
evolution from the metazoan and fungal lineages and have developed distinct 
mechanisms in gene expression and other molecular processes, which are not only 
interesting from a mechanistic point of view, but which also have the potential 
to being exploited for anti-parasitic therapy. Based on a multidisciplinary 
approach including x-ray crystallography, x-ray footprinting, and mass 
spectrometry, I will present a mechanism of histone H3 lysine K76 methylation 
by T. brucei DOT1 enzymes distinct from that of human and yeast homologs, 
providing insight into the evolution, regulation, and function of kinetoplastid 
DOT1 methyltransferases.



==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e nsls.lifescien...@gmail.com

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973





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[ccp4bb] CBMS Lecture Series - Erik Debler - January 24; 13:30 (EST)

[Stojanoff, Vivian]

You are cordially invited to join  the Center for Biomolecular Structure 
Lecture Series ………..





Erik Debler

Thomas Jefferson University



WEDNESDAY, January 24, 13:30 (EST)





"Hybrid methods to investigate the mechanism of Dot1 histone-modifying enzymes 
in kinetoplastid parasites"



Register in advance for this meeting:



 https://bnl.zoomgov.com/meeting/register/vJItcu2grTotGGdsWXVwtDa4OIkqHcJgvpA



Time conversion Link: 
https://www.worldtimebuddy.com/



Abstract: Kinetoplastid parasites are medically important eukaryotes that are 
responsible for severe neglected tropical diseases including sleeping sickness 
caused by Trypanosoma brucei. Kinetoplastids have diverged early on in 
evolution from the metazoan and fungal lineages and have developed distinct 
mechanisms in gene expression and other molecular processes, which are not only 
interesting from a mechanistic point of view, but which also have the potential 
to being exploited for anti-parasitic therapy. Based on a multidisciplinary 
approach including x-ray crystallography, x-ray footprinting, and mass 
spectrometry, I will present a mechanism of histone H3 lysine K76 methylation 
by T. brucei DOT1 enzymes distinct from that of human and yeast homologs, 
providing insight into the evolution, regulation, and function of kinetoplastid 
DOT1 methyltransferases.



==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e nsls.lifescien...@gmail.com

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973



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[ccp4bb] CBMS Lecture Series - December 13, 13:30 (EST) - Dr Hui-Ling (Sunny) Liao

[Stojanoff, Vivian]

You and your team are invited to join ……..







Hui-Ling (Sunny) Liao



SWES, NFREC/University of Florida



Wednesday, December 13, 2023, 13:30 EST



Exploring symbiome-mediated territorial nutrient processes and environmental 
adaptation through the Pinus-Suillus Model



  Virtual - Register   



https://bnl.zoomgov.com/meeting/register/vJItduqprD0uGqG36q9v45J5p9n5Ycxws64



Abstract

Forest ecosystems, encompassing 30% of the Earth’s land area, possess 
significant C storage capabilities, regulate and store ~50 billion tons of soil 
organic matter. Its capacity makes forest as vital players in climate change 
mitigation.Over millions of years, forest trees and their symbiotic partners, 
such as the key stone symbiotic fungi Suillus, have co-evolved intricate 
mechanisms to support each other in nutrient acquisition and adaptation to 
dynamic environments, including biotic and abiotic stresses. Using Pinus and 
Suillus as a model, our research aims at unveiling the communication and 
regulation mechanisms employed by plants and their symbionts, facilitating 
nutrient flux and adaptation to evolving environments. Our investigative tools 
include metagenomic, metatranscriptomic, metaproteomic, and metabolomic 
analyses, coupled with biogeochemical and chemical imaging approaches. This 
presentation provides an overview of our ongoing projects examining 
Pinus-Suillus-soil interactions and their consequences on nutrient allocation 
and stress environment adaptation. We will emphasize the application of X-ray 
imaging technology in elucidating these intricate mechanisms.

===



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e nsls.lifescien...@gmail.com

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973



Supporting Grants: CBMS is supported by NIH-NIGMS and by the DOE-BER. Any work 
performed at NSLS-II is supported by DOE-BES under contract # DE-SC0012704.





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[ccp4bb] CBMS Lecture Series - Professor Mario E Rivera - October 25, 13:30 (EST) - "Antibiofilm"

[Stojanoff, Vivian]

You are cordially invited to join ……..   



Mario E. Rivera



Professor and William A. Pryor

Chair Department of Chemistry

Louisiana State University





Wednesday, October 25, 2023, 13:30 EDT



Manipulating iron storage and mobilization in the bacterial cell, a new 
strategy for developing antibiofilm





https://bnl.zoomgov.com/meeting/register/vJItd-6tqz0vEgchVuS3Ax9XRXZRcYlZKi0






Abstract

Biofilm-embedded cells can be up to 1000-fold more tolerant to antibiotic 
treatment than planktonic cells. Antibiotic tolerance is a condition which does 
not involve mutation and enables bacteria to survive in the presence of 
antibiotics. The antibiotic tolerance of biofilm-cells often renders 
antibiotics ineffective, even against bacterial strains that do not carry 
resistance-imparting mutations. A key component of iron metabolism is the 
storage of Fe(III) in bacterioferritin and its subsequent mobilization as 
Fe(II) to satisfy metabolic requirements. In P. aeruginosa, the mobilization of 
Fe(III) from bacterioferritin (Bfr) to the cytosol requires binding of a 
ferredoxin (Bfd) to reduce the stored Fe(III) and release it as the soluble 
Fe(II). This presentation will discuss evidence showing that deletion of the 
bfd gene triggers an irreversible accumulation of Fe(III) in BfrB, concomitant 
intracellular iron deficiency, metabolic dysregulation, and impaired biofilm 
development. The treatment of Pseudomonas aeruginosa mature biofilms with 
recently discovered small molecule inhibitors of the BfrB-Bfd complex kills 
biofilm-entrenched cells. The conservation of Bfr and Bfd amino acid sequences 
fromP. aeruginosa, Acinetobacter baumannii, and Klebsiella pneumoniae suggest 
the inhibitors may also be active against these pathogens, and susceptibility 
testing experiments with A. baumannii support this idea.





===



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e nsls.lifescien...@gmail.com

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973



Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.





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[ccp4bb] CBMS Structural Biology Workbench - November 13 to 16, 2023

[Stojanoff, Vivian]

Dear All,


We'd like to invite you to register for the CBMS Structural Biology Workbench 
schedule

November 13 through 16. Participants can choose between SAXS and

MX or attend both. The event will be  held virtually.


Registration is free:


https://www.bnl.gov/cbmsworkbench/

Kind regards,

Vivian Stojanoff

--
Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
p 1(631) 344 8375
e nsls.lifescien...@gmail.com<mailto:nsls.lifescien...@gmail.com>
w https://www.bnl.gov/ps/lifesciences/<https://www.bnl.gov/ps/lsbr/>

Address:
Center for Biomolecular Structure
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973

Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES
under contract # DE-SC0012704.




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[ccp4bb] Reminder: CBMS Lecture Series - September 20 - 1:30 pm - Amir Khan

[Stojanoff, Vivian]

 You are cordially invited to join ……..   



Amir Khan



Trinity College Dublin



Wednesday, September 20, 2023, 13:30 EDT



Structural biology of phospho-dependent signaling in the context of LRRK2 
kinase and Parkinson’s disease



https://bnl.zoomgov.com/meeting/register/vJIsfu6vqzkvHaKAt9fDIW--AHKPN8yemIw



Abstract

Activation of LRRK2 kinase activity has long been associated with inherited and 
sporadic forms of Parkinson’s disease. However, the molecular basis for the 
defects in subsequent cell signaling that lead to neuronal cell death remain 
unknown. LRRK2 phosphorylates numerous Rab small GTPases and takes control of 
their functions in the regulation of vesicular and membrane trafficking. Here I 
will discuss how LRRK2 affects downstream cell signaling complexes using 
biophysical and structural techniques.  These studies contribute to our 
understanding of how LRRK2-mediated phopshorylation is linked to 
neurodegeneration in the context of Parkinson’s disease.



===



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e nsls.lifescien...@gmail.com

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973



Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.





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[ccp4bb] CBMS Lecture Series - September 20 - 1:30 pm - Amir Khan

[Stojanoff, Vivian]

You are cordially invited to join ……..   



Amir Khan



Trinity College Dublin



Wednesday, September 20, 2023, 13:30 EDT



Structural biology of phospho-dependent signaling in the context of LRRK2 
kinase and Parkinson’s disease



https://bnl.zoomgov.com/meeting/register/vJIsfu6vqzkvHaKAt9fDIW--AHKPN8yemIw



Abstract

Activation of LRRK2 kinase activity has long been associated with inherited and 
sporadic forms of Parkinson’s disease. However, the molecular basis for the 
defects in subsequent cell signaling that lead to neuronal cell death remain 
unknown. LRRK2 phosphorylates numerous Rab small GTPases and takes control of 
their functions in the regulation of vesicular and membrane trafficking. Here I 
will discuss how LRRK2 affects downstream cell signaling complexes using 
biophysical and structural techniques.  These studies contribute to our 
understanding of how LRRK2-mediated phopshorylation is linked to 
neurodegeneration in the context of Parkinson’s disease.



===



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e nsls.lifescien...@gmail.com

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973



Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.





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[ccp4bb] Reminder: CBMS Lecture Series - August 16 13:30 (EDT) - Jochen Zimmer

[Stojanoff, Vivian]

You are cordially invited to join ……..



Jochen Zimmer


 Professor, Molecular Physiology and 
Biological Physics
  
School of Medicine
     
University of Virginia



  Wednesday, August 16, 2023, 13:30 EDT


  Molecular insights into polysaccharide secretion by ABC 
transporters



 
https://bnl.zoomgov.com/meeting/register/vJItc-ysqj0oGZ57YFYVzEYm4se7kgZo66E  




Abstract

O antigens are ubiquitous protective extensions of lipopolysaccharides in the 
extracellular leaflet of the gram-negative outer membrane. Following 
biosynthesis in the cytosol, the lipid-linked polysaccharide is transported to 
the periplasm by the WzmWzt ABC transporter. Often, O antigen secretion 
requires the chemical modification of its elongating terminus, which the ABC 
transporter recognizes via a carbohydrate-binding domain (CBD). We identified 
that methylated mannose or rhamnose caps the O antigen of Aquifex aeolicus. 
Crystal and cryo electron microscopy structures reveal how WzmWzt recognizes 
this cap between its carbohydrate and nucleotide-binding domains in a 
nucleotide-free state. ATP binding induces drastic conformational changes of 
its CBD, terminating interactions with the O antigen. Combined with mutagenesis 
and functional analyses, our results elucidate critical steps in the 
recognition and translocation of polysaccharides by ABC transporters.



===



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e nsls.lifescien...@gmail.com

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973



Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.




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[ccp4bb] Reminder CBMS Lecture Series - Carolyn Larabell - 13:30 (EDT)

[Stojanoff, Vivian]

You are cordially invited to join ……..



Carolyn Larabell


Professor, University of California San Francisco

Faculty Scientist, Lawrence Berkeley National Laboratory



Wednesday, July 19, 2023, 13:30 EDT (New York time)


Soft X-ray Tomography:  Quantitative Structural Cell Biology at the Mesoscale




 
https://bnl.zoomgov.com/meeting/register/vJItdeyrrTkoGfb4oMXZMF9r_J58cZ_Dfd0


Abstract

Soft X-ray tomography (SXT) is similar in concept to the well-established 
medical diagnostic technique, computed axial tomography (CAT), except SXT is 
capable of imaging single cells up to 20 µm diameter with a spatial resolution 
of 35 nm or better. Cells are simply rapidly frozen, placed in a goniometer, 
and imaged through 360 degrees to achieve isotropic resolution. Cells imaged by 
SXT are, therefore, highly representative of the cell in its native, functional 
state. Cells are illuminated with x-ray photons from within a region of the 
spectrum known as the 'water window' (284 – 543eV). 'Water window' x-ray 
photons are absorbed an order of magnitude more strongly by carbon- and 
nitrogen-containing organic material than by water. Consequently, variation in 
biomolecule composition and concentration gives rise to quantitative, 
high-contrast images of intact, fully hydrated cells without the need to use 
contrast-enhancing agents. Attenuation of soft x-rays as they pass through the 
specimen adheres to the Beer-Lambert Law, yielding unique quantitative Linear 
Absorption Coefficient (LAC) measurements for cellular components. 
Three-dimensional images of an entire cell can be obtained in about ten 
minutes, enabling analyses of large number of cells with multiple 
manipulations. At the National Center for X-ray Tomography in Berkeley 
California, we are working with a large number of scientists from around the 
world to image a variety of different cell types. I will present highlights of 
some of these projects to demonstrate the unique information that can be 
generated by SXT and the broad spectrum of biological applications.





===



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e nsls.lifescien...@gmail.com

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973



Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.





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hosted by www.jiscmail.ac.uk, terms & conditions are available at 
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[ccp4bb] CBMS Lecture Series - Carolyn Larabell - July 19, 13:30 (EDT)

[Stojanoff, Vivian]

You are cordially invited to join ……..



Caroline Larabell


Professor, University of California San Francisco

Faculty Scientist, Lawrence Berkeley National Laboratory



Wednesday, July 19, 2023, 13:30 EDT (New York time)


Soft X-ray Tomography:  Quantitative Structural Cell Biology at the Mesoscale




 
https://bnl.zoomgov.com/meeting/register/vJItdeyrrTkoGfb4oMXZMF9r_J58cZ_Dfd0


Abstract

Soft X-ray tomography (SXT) is similar in concept to the well-established 
medical diagnostic technique, computed axial tomography (CAT), except SXT is 
capable of imaging single cells up to 20 µm diameter with a spatial resolution 
of 35 nm or better. Cells are simply rapidly frozen, placed in a goniometer, 
and imaged through 360 degrees to achieve isotropic resolution. Cells imaged by 
SXT are, therefore, highly representative of the cell in its native, functional 
state. Cells are illuminated with x-ray photons from within a region of the 
spectrum known as the 'water window' (284 – 543eV). 'Water window' x-ray 
photons are absorbed an order of magnitude more strongly by carbon- and 
nitrogen-containing organic material than by water. Consequently, variation in 
biomolecule composition and concentration gives rise to quantitative, 
high-contrast images of intact, fully hydrated cells without the need to use 
contrast-enhancing agents. Attenuation of soft x-rays as they pass through the 
specimen adheres to the Beer-Lambert Law, yielding unique quantitative Linear 
Absorption Coefficient (LAC) measurements for cellular components. 
Three-dimensional images of an entire cell can be obtained in about ten 
minutes, enabling analyses of large number of cells with multiple 
manipulations. At the National Center for X-ray Tomography in Berkeley 
California, we are working with a large number of scientists from around the 
world to image a variety of different cell types. I will present highlights of 
some of these projects to demonstrate the unique information that can be 
generated by SXT and the broad spectrum of biological applications.





===



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e nsls.lifescien...@gmail.com

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973



Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.





To unsubscribe from the CCP4BB list, click the following link:
https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB=1

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[ccp4bb] REMINDER: CBMS Lecture Series - Dominique Bourgeois - June 28, 13:30

[Stojanoff, Vivian]

You are cordially invited to join ……..



Dominique Bourgeois


Institut de Biologie Structurale J-P. Ebel, GRENOBLE



Wednesday, June 28, 2023, 13:30 EDT (New York time)



STRUCTURAL PHOTOPHYSICS OF FLUORESCENT PROTEINS USED IN SUPER RESOLUTION 
MICROSCOPY


https://bnl.zoomgov.com/meeting/register/vJIsf-2orTkoHue9RhbBuN5K0UKRrafNNTk



Abstract

Phototransformable fluorescent proteins (PTFPs) are widely used in many 
advanced fluorescence microscopy methods, notably in the super-resolution 
field. A plethora of PTFPs have been engineered in the last years, which 
display a variety of photoactivation, photoconversion, photoswitching, 
photoblinking and photobleaching properties that can be used at advantage in 
many super-resolution schemes, but that are also at the origin of significant 
complications and artifacts, making these fascinating genetically encoded 
labels still far from ideal. In this talk, I will review how (kinetic) X-ray 
crystallography, optical spectroscopy, multidimensional NMR and molecular 
dynamics simulations can be combined with single-molecule investigations to 
reveal phototransformation mechanisms of PTFPs at the near-atomic level.



 Graphical Abstract:


[cid:653945e9-d41c-4f3d-bb0a-2b57aba4efed]



===



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e nsls.lifescien...@gmail.com

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973



Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.





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[ccp4bb] CBMS Lecture Series - Dominique Bourgeois - June 28, 13:30

[Stojanoff, Vivian]

You are cordially invited to join ……..



Dominique Bourgeois


Institut de Biologie Structurale J-P. Ebel, GRENOBLE



Wednesday, June 28, 2023, 13:30 EDT (New York time)



STRUCTURAL PHOTOPHYSICS OF FLUORESCENT PROTEINS USED IN SUPER RESOLUTION 
MICROSCOPY


https://bnl.zoomgov.com/meeting/register/vJIsf-2orTkoHue9RhbBuN5K0UKRrafNNTk



Abstract

Phototransformable fluorescent proteins (PTFPs) are widely used in many 
advanced fluorescence microscopy methods, notably in the super-resolution 
field. A plethora of PTFPs have been engineered in the last years, which 
display a variety of photoactivation, photoconversion, photoswitching, 
photoblinking and photobleaching properties that can be used at advantage in 
many super-resolution schemes, but that are also at the origin of significant 
complications and artifacts, making these fascinating genetically encoded 
labels still far from ideal. In this talk, I will review how (kinetic) X-ray 
crystallography, optical spectroscopy, multidimensional NMR and molecular 
dynamics simulations can be combined with single-molecule investigations to 
reveal phototransformation mechanisms of PTFPs at the near-atomic level.



 Graphical Abstract:


[cid:653945e9-d41c-4f3d-bb0a-2b57aba4efed]



===



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e nsls.lifescien...@gmail.com

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973



Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.





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SUMMARY:CBMS Lecture Series - Bourgeois
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[ccp4bb] Reminder >>> CBMS Lecture Series - May 17 13:30 (EDT)

[Stojanoff, Vivian]

You are cordially invited to join ……..



Jin Kim Montclare


Director of the Convergence for Innovation and Entrepreneurship (CIE) Institute

Chemical and Biomolecular Engineering & Biomedical Engineering, NYU Tandon 
School of Engineering

Chemistry, NYU College of Arts & Sciences



Wednesday, May 17, 2023, 13:30 EDT


Responsive Protein Engineered Biomaterials





https://bnl.zoomgov.com/meeting/register/vJIsc-qtqDstGpkgng2VJupNtdgPwDtp1ys





Abstract

Inspired by nature’s biopolymers, we engineer artificial protein materials with 
entirely new properties and function.  We employ synthetic and chemical biology 
to construct our materials and endow them with stimuli-responsiveness. In 
particular, we have fabricated protein-derived nanomaterials: coiled-coil 
fibers, helix-elastin block polymers, and supercharged coiled-coil•lipid 
complexes (or lipoproteoplexes).  We investigate the fundamental self-assembly 
and molecular recognition capabilities of these systems.  More importantly, we 
are able to harness these structure as well as others to interface with small 
molecule therapeutics, genes, and cells.



===



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e nsls.lifescien...@gmail.com

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973



Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.




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[ccp4bb] CBMS Lecture Series - Jin Montclare - May 17 13:30 (EDT)

[Stojanoff, Vivian]

You and your team are invited to join ……..



Jin Kim Montclare

Director of the Convergence for Innovation and Entrepreneurship (CIE) Institute

Chemical and Biomolecular Engineering & Biomedical Engineering, NYU Tandon 
School of Engineering

Chemistry, NYU College of Arts & Sciences



Wednesday, May 17, 2023, 13:30 EDT


Responsive Protein Engineered Biomaterials



https://bnl.zoomgov.com/meeting/register/vJIsc-qtqDstGpkgng2VJupNtdgPwDtp1ys





Abstract

Inspired by nature’s biopolymers, we engineer artificial protein materials with 
entirely new properties and function.  We employ synthetic and chemical biology 
to construct our materials and endow them with stimuli-responsiveness. In 
particular, we have fabricated protein-derived nanomaterials: coiled-coil 
fibers, helix-elastin block polymers, and supercharged coiled-coil•lipid 
complexes (or lipoproteoplexes).  We investigate the fundamental self-assembly 
and molecular recognition capabilities of these systems.  More importantly, we 
are able to harness these structure as well as others to interface with small 
molecule therapeutics, genes, and cells.



===



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e nsls.lifescien...@gmail.com

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973



Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.












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[ccp4bb] NSLS II User Meeting - New Science Enabled by UTH Crystallography

[Stojanoff, Vivian]

Dear All

We would like to call your attention to the NSLS II workshop "New Science 
Enabled by Ultra-high Throughput 
Crystallography" on 
April 28.  This is an opportunity for the community to discuss next-generation 
science and to define the requirements for next-generation instrumentation 
needed for this science.  External speakers will discuss topics such as the 
SARS CoV 2 Macrodomain (Fraser group), protein dynamics and fragment screening 
(Page group), and metabolite and effector binding for biofuel development (Jez 
group).  NSLS 2 staff will describe potential instrumentation that could enable 
your science.  Make your voice heard today, to assure you have the resources 
you need tomorrow!  Registration  
for this virtual cost-free meeting is open now.  We hope to see you in two 
weeks!

Agenda:
https://www.bnl.gov/usersmeeting/files/pdf/agenda.pdf

Registration is required & FREE:
https://www.bnl.gov/usersmeeting/index.php



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[ccp4bb] CBMS workbench: Structural Biology

[Stojanoff, Vivian]

Dear All,

We'd like to bring to your attention that the registration is open for the CBMS 
Structural Biology Workbench, scheduled May 15 through May 18.  Participants 
can choose between SAXS and MX or attend both. The event will be held 
virtually.  Registration is free:

https://www.bnl.gov/cbmsworkbench/

Kind regards,

Vivian

--
Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
p 1(631) 344 8375
e nsls.lifescien...@gmail.com
w https://www.bnl.gov/ps/lifesciences/

Address:
Center for Biomolecular Structure
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973

Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.





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[ccp4bb] CBMS Workbench: Structural Biology

[Stojanoff, Vivian]

Dear All,

We'd like to bring to your attention that the registration is open for the CBMS 
Structural Biology Workbench, scheduled May 15 through May 18.  Participants 
can choose between SAXS and MX or attend both. The event will be held 
virtually.  Registration is free:

https://www.bnl.gov/cbmsworkbench/

Kind regards,

Vivian

--
Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
p 1(631) 344 8375
e nsls.lifescien...@gmail.com
w https://www.bnl.gov/ps/lifesciences/

Address:
Center for Biomolecular Structure
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973

Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.





To unsubscribe from the CCP4BB list, click the following link:
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[ccp4bb] NSLS II User Meeting - Workshop April 28 @ 9:45 AM

[Stojanoff, Vivian]

We like to call your attention to the NSLS2 User Meeting workshop "New Science 
Enabled by Ultra-high Throughput 
Crystallography" on 
April 28.  This is an opportunity for the community to discuss the 
next-generation science and to define the instrumentation that will enable  
this science.  Invited speakers will discuss topics such as the SARS CoV 2 
Macrodomain (Fraser group), protein dynamics and fragment screening (Page 
group), and metabolite and effector binding for biofuel development (Jez 
group).  NSLS 2 staff will describe potential instrumentation that could enable 
your science.  Make your voice heard today, to assure you have the resources 
you need tomorrow!  Registration  
for this virtual cost-free meeting is open now.  We hope to see you in two 
weeks!

Agenda:
https://www.bnl.gov/usersmeeting/files/pdf/agenda.pdf

Registration:
https://www.bnl.gov/usersmeeting/index.php



Wuxian Shi and Alex Soares
Organizers
Center for Biomolecular Structure (CBMS)





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[ccp4bb] CBMS Lecture Series - March 22 @13:30 (EST) - Diana Monteiro (HWI)

[Stojanoff, Vivian]

You and your team are invited to join

Diana Monteiro

Hauptman-Woodward Medical Research
NSF BioXFEL Science and Technology Center

March 22, 13:30 EST

Beyond cryo-crystallography: new technologies for serial and time-resolved 
experiments

https://bnl.zoomgov.com/meeting/register/vJItc-qgqTkrEvDDy1Koep3o6jrqajWyhRY


Abstract
The advent of cryocrystallography made determining the high resolution of 
proteins using X-ray diffraction truly possible by reducing radiation damage of 
the samples. It is still the most widely used method, accounting for the vast 
majority of structures currently in the Protein Data Bank. But, with the advent 
of brighter X-ray sources (third and fourth generation synchrotrons and X-ray 
free electron lasers), the number of room temperature (RT), protein structures 
determined by X-ray diffraction is increasing once more. The development of 
technologies towards serial crystallography, including sample preparation, 
delivery, hardware and software advances, make these studies possible. RT 
structures show variations in conformations, highlighting structure-function 
relationships important for basic science and drug discovery. In this talk I 
will give an overview of some of the technologies and techniques we have worked 
on in recent years, including their application towards time-resolved 
experiments.

==
Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
p 1(631) 344 8375
e nsls.lifescien...@gmail.com
w https://www.bnl.gov/ps/lifesciences/

Address:
Center for Biomolecular Structure
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973

Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.





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[ccp4bb] CBMS Workbench Structural Biology - January 31st to February 2nd

[Stojanoff, Vivian]

Dear Colleagues,

We'd like to bring to your attention that the registration is open for the CBMS 
Structural Biology Workbench, scheduled January 31st through February 2nd.  
Participants can choose between SAXS and MX or attend both. The event will be 
held virtually.  Registration is free:

https://www.bnl.gov/cbmsworkbench/

Kind regards,

Vivian

--
Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
p 1(631) 344 8375
e nsls.lifescien...@gmail.com
w https://www.bnl.gov/ps/lifesciences/

Address:
Center for Biomolecular Structure
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973

Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.




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[ccp4bb] Fw: CBMS Lecture Series - January 18, 2023; 13:30 (EST)

[Stojanoff, Vivian]

You are cordially invited to join  the Center for Biomolecular Structure 
Lecture Series ………..



Amir Khan


Associate Professor

Trinity College Dublin

WEDNESDAY, JANUARY 18, 13:30 (EST)



"PPM1H phosphatase specificity for Rab GTPases"



Register in advance for this meeting:

https://bnl.zoomgov.com/meeting/register/vJIsceugqDwoGHSNUX28x5ZhdmleK_hkPVw​​



Time conversion Link: 
https://www.worldtimebuddy.com/



Abstract:

LRRK2 serine/threonine kinase is associated with inherited Parkinson’s disease. 
LRRK2 phosphorylates a subset of Rab GTPases within their switch 2 motif to 
control their interactions with effectors. Recent work has shown that the 
metal-dependent protein phosphatase PPM1H counteracts LRRK2 by 
dephosphorylating Rabs. PPM1H is highly selective for LRRK2 phosphorylated 
Rabs, and closely related PPM1J exhibits no activity toward substrates such as 
Rab8a. We have identified the structural determinant of PPM1H specificity for 
Rabs. The crystal structure of PPM1H reveals a conserved catalytic domain 
punctuated by a 110-residue flap domain adjacent to the active site. 
Biochemical and cellular assays suggest that the flap domain of PPM1H encodes 
the docking motif for phosphorylated Rabs.





Bio:

Amir Khan graduated with a PhD from the University of Alberta, Canada. He 
performed post-doctoral work with Don Wiley at Harvard University, and also 
with Anne Houdusse at Institut Curie, Paris. It was in Paris that he became 
interested in Rab GTPases and their interactions with effector proteins.  In 
recent years, he has become interested in how Rab control of membrane 
trafficking intersects with neurodegeneration in the context of Parkinson’s 
disease. He recently joined Trinity College at Dublin. Associate Professor  at 
Trinity College Dublin





==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e lifesciences@bnl.gov

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973




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[ccp4bb] Reminder: CBMS Lecture Series - January 18, 2023 @ 13:30 (EST)

[Stojanoff, Vivian]

https://bnl.zoomgov.com/meeting/register/vJIsceugqDwoGHSNUX28x5ZhdmleK_hkPVw

You are cordially invited to join  the Center for Biomolecular Structure 
Lecture Series ………..



Amir Khan


Associate Professor

Trinity College Dublin

WEDNESDAY, JANUARY 18, 13:30 (EST)



"PPM1H phosphatase specificity for Rab GTPases"



Register in advance for this meeting:

https://bnl.zoomgov.com/meeting/register/vJIsceugqDwoGHSNUX28x5ZhdmleK_hkPVw​​



Time conversion Link: 
https://www.worldtimebuddy.com/



Abstract:

LRRK2 serine/threonine kinase is associated with inherited Parkinson’s disease. 
LRRK2 phosphorylates a subset of Rab GTPases within their switch 2 motif to 
control their interactions with effectors. Recent work has shown that the 
metal-dependent protein phosphatase PPM1H counteracts LRRK2 by 
dephosphorylating Rabs. PPM1H is highly selective for LRRK2 phosphorylated 
Rabs, and closely related PPM1J exhibits no activity toward substrates such as 
Rab8a. We have identified the structural determinant of PPM1H specificity for 
Rabs. The crystal structure of PPM1H reveals a conserved catalytic domain 
punctuated by a 110-residue flap domain adjacent to the active site. 
Biochemical and cellular assays suggest that the flap domain of PPM1H encodes 
the docking motif for phosphorylated Rabs.





Bio:

Amir Khan graduated with a PhD from the University of Alberta, Canada. He 
performed post-doctoral work with Don Wiley at Harvard University, and also 
with Anne Houdusse at Institut Curie, Paris. It was in Paris that he became 
interested in Rab GTPases and their interactions with effector proteins.  In 
recent years, he has become interested in how Rab control of membrane 
trafficking intersects with neurodegeneration in the context of Parkinson’s 
disease. He recently joined Trinity College at Dublin. Associate Professor  at 
Trinity College Dublin





==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e lifesciences@bnl.gov

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973







To unsubscribe from the CCP4BB list, click the following link:
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[ccp4bb] Reminder: CBMS Lecture Series - December 14 13:30 (EST)

[Stojanoff, Vivian]

You are cordially invited to join  the Center for Biomolecular Structure 
Lecture Series ………..



Andres Finzi


Canada Research Chair on Retroviral Entry

Member of The College of the Royal Society of Canada

Associate Professor, Faculty of Medicine, Université de Montréal



WEDNESDAY, December 14, 13:30 (EST)



"Modulating HIV-1 Env conformation to eliminate infected cells"



Register in advance for this meeting:

 https://bnl.zoomgov.com/meeting/register/vJItcO6hrTMpGQ0PHGXLvZgC2gWbXrF4-3I​​



Time conversion Link: 
https://www.worldtimebuddy.com/



Abstract:

HIV-1 evolved to conceal its envelope glycoproteins (Env) from recognition by 
antibodies elicited in most infected individuals.  This lack of recognition 
translates into a lack of neutralization.  Therefore, these antibodies are 
known as non-neutralizing antibodies (nnAbs).  However, antibodies have several 
functions beyond neutralization, with Fc-effector functions being scrutinized 
in the last few years.  Unfortunately, nnAbs also fail to eliminate infected 
cells due to their incapacity to recognize Env.  We developed a new strategy to 
“open up” Env at the surface of infected cells thus enabling recognition by 
nnAbs.  This approach renders infected cells susceptible to antibody-dependent 
cellular cytotoxicity (ADCC) and therefore it could represent a new tool to 
achieve a functional cure.



Bio:

Dr. Finzi is Associate Professor and Canada Research Chair on Retroviral Entry 
at Université de Montréal.  Dr Finzi is a leader in HIV-1 envelope glycoprotein 
conformational changes, accessory proteins and Fc-mediated effector functions.  
His work has important implications for the development of new therapeutic 
strategies to fight HIV-1.  The excellence of Dr Finzi’s research program has 
been recognized by several distinctions and awards.  Since November 2020 he is 
a Member of The College of the Royal Society of Canada.





==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e lifesciences@bnl.gov

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973






To unsubscribe from the CCP4BB list, click the following link:
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BEGIN:VCALENDAR
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DTSTART;TZID=America/New_York:20221214T133000
DTEND;TZID=America/New_York:20221214T143000
SUMMARY:CBMS Lecture Series  - Andres Finzi
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 6835\nOne tap mobile\n+16692545252\,\,1607793833#\,\,\,\,*346835# US (Sa
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 al by your location\n+1 669 254 5252 US (San Jose)\n+1 6
 46 828 7666 US (New York)\n+1 669 216 1590 US (San Jose)\n  
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 mRUdSdz09

[ccp4bb] CBMS "Office Hour" December 12

[Stojanoff, Vivian]

Dear All

In preparation to the APS shutdown between April 2023 and May 2024 we organize 
the "CBMS Office hour" to answer eventual questions  from the MX and SAXS 
communities, interested in learning more about the NSLS II beam lines.

To join the  "CBMS Office Hour" Monday December 12 at noon (EST). Please do 
register:

 https://bnl.zoomgov.com/meeting/register/vJIsf-iurD8iHvar9lh_oxQz0yUZlh4fnXU

These meetings are informal and intended to clarify any questions the community 
may have.

NEXT DEADLINE for PROPOSAL submissions for beam time May - August 2023 is 
JANUARY 31st 2023.

Kind regards

Vivian


==

Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e lifesciences@bnl.gov

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure (CBMS)

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973



Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.





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PRODID:-//zoom.us//iCalendar Event//EN
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METHOD:PUBLISH
CLASS:PUBLIC
BEGIN:VTIMEZONE
TZID:America/New_York
LAST-MODIFIED:20221105T024526Z
TZURL:http://www.tzurl.org/zoneinfo-outlook/America/New_York
X-LIC-LOCATION:America/New_York
BEGIN:DAYLIGHT
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 ng.\n\nJoin ZoomGov Meeting\nhttps://bnl.zoomgov.com/j/1618162484?pwd=QX
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 1599\nOne tap mobile\n+16692545252\,\,1618162484#\,\,\,\,*181599# US (Sa
 n Jose)\n+16468287666\,\,1618162484#\,\,\,\,*181599# US (New York)\n\nDi
 al by your location\n+1 669 254 5252 US (San Jose)\n+1 6
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 tYS9rdz09
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[ccp4bb] CBMS Lecture Series - Andres Finzi on HIV

[Stojanoff, Vivian]

You are cordially invited to join  the Center for Biomolecular Structure 
Lecture Series ………..



Andres Finzi

Canada Research Chair on Retroviral Entry
Member of The College of the Royal Society of Canada
Associate Professor, Faculty of Medicine, Université de Montréal


WEDNESDAY, December 14, 13:30 (EST)



"Modulating HIV-1 Env conformation to eliminate infected cells"



Register in advance for this meeting:

 https://bnl.zoomgov.com/meeting/register/vJItcO6hrTMpGQ0PHGXLvZgC2gWbXrF4-3I​​



Time conversion Link: 
https://www.worldtimebuddy.com/



Abstract:
HIV-1 evolved to conceal its envelope glycoproteins (Env) from recognition by 
antibodies elicited in most infected individuals.  This lack of recognition 
translates into a lack of neutralization.  Therefore, these antibodies are 
known as non-neutralizing antibodies (nnAbs).  However, antibodies have several 
functions beyond neutralization, with Fc-effector functions being scrutinized 
in the last few years.  Unfortunately, nnAbs also fail to eliminate infected 
cells due to their incapacity to recognize Env.  We developed a new strategy to 
“open up” Env at the surface of infected cells thus enabling recognition by 
nnAbs.  This approach renders infected cells susceptible to antibody-dependent 
cellular cytotoxicity (ADCC) and therefore it could represent a new tool to 
achieve a functional cure.



Bio:
Dr. Finzi is Associate Professor and Canada Research Chair on Retroviral Entry 
at Université de Montréal.  Dr Finzi is a leader in HIV-1 envelope glycoprotein 
conformational changes, accessory proteins and Fc-mediated effector functions.  
His work has important implications for the development of new therapeutic 
strategies to fight HIV-1.  The excellence of Dr Finzi’s research program has 
been recognized by several distinctions and awards.  Since November 2020 he is 
a Member of The College of the Royal Society of Canada.





==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e lifesciences@bnl.gov

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973






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BEGIN:VEVENT
DTSTAMP:20221122T192519Z
DTSTART;TZID=America/New_York:20221214T133000
DTEND;TZID=America/New_York:20221214T143000
SUMMARY:CBMS Lecture Series  - Andres Finzi
UID:20221122T192519Z-1607793833@fe80:0:0:0:4f3:3aff:fe13:dd60eth0
TZID:America/New_York
DESCRIPTION:Vivian Stojanoff is inviting you to a scheduled ZoomGov meeti
 ng.\n\nJoin ZoomGov Meeting\nhttps://bnl.zoomgov.com/j/1607793833?pwd=N2
 JSOGF0cGQ1MU9EOXR6RktmRUdSdz09\n\nMeeting ID: 160 779 3833\nPasscode: 34
 6835\nOne tap mobile\n+16692545252\,\,1607793833#\,\,\,\,*346835# US (Sa
 n Jose)\n+16468287666\,\,1607793833#\,\,\,\,*346835# US (New York)\n\nDi
 al by your location\n+1 669 254 5252 US (San Jose)\n+1 6
 46 828 7666 US (New York)\n+1 669 216 1590 US (San Jose)\n  
   +1 551 285 1373 US\nMeeting ID: 160 779 3833\nPasscode: 346835\nFind y
 our local number: https://bnl.zoomgov.com/u/ad3yT9x0JS\n\nJoin by SIP\n1
 607793...@sip.zoomgov.com\n\nJoin by H.323\n161.199.138.10 (US West)\n16
 1.199.136.10 (US East)\nMeeting ID: 160 779 3833\nPasscode: 346835\n\n
LOCATION:https://bnl.zoomgov.com/j/1607793833?pwd=N2JSOGF0cGQ1MU9EOXR6Rkt
 mRUdSdz09

[ccp4bb] Fw: CBMS Lecture Series - David Harper - "Engineered Carbon Materials Derived from Lignin for Energy Storage" - TODAY !!!!! November 16, 13:30 (EST - NYC time zone)

[Stojanoff, Vivian]

You are cordially invited to join  the Center for Biomolecular Structure 
Lecture Series ………..



David P. Harper

Center for Renewable Carbon, The University of Tennessee

WEDNESDAY, November 16, 13:30 (EST)



"Engineered Carbon Materials Derived from Lignin for Energy Storage"



Register in advance for this meeting:
  https://bnl.zoomgov.com/meeting/register/vJIsf-GuqjkvHvUBsoAXXwWoAjcRqXR8BPA​​



  Time conversion Link: 
https://www.worldtimebuddy.com/



Abstract:

Lignin’s carbon-dense aromatic structure and abundance promise to replace 
carbon derived from fossil or mined sources. However, lignin’s heterogeneous, 
amorphous structure and difficulty isolating it in high purity from woody 
feedstocks make predicting processing performance and carbon structure 
difficult. Strategies for processing multiple lignin feedstocks from 
organosolv, kraft, and other fractionation technologies into carbon materials, 
along with the relative advantages/disadvantages of carbon from traditional 
sources. Further, the influence of processing and lignin sources on the 
development of carbon structure will be addressed. Preliminary models for 
lignin-based carbon materials will be presented along with potential 
implications for their use in energy storage and beyond.



Bio:

Dr. Harper earned a BA in Physics from West Virginia University and a Ph.D. in 
Civil Engineering from Washington State University in 2003, focusing on 
structural composite materials. He was a Post-Doctoral Fellow at the USDA 
Forest Products Laboratory in Madison, WI. Dr. Harper joined the Department of 
Forestry, Wildlife, and Fisheries in 2004 at the University of Tennessee 
located within UT’s Institute of Agriculture and is a joint faculty member in 
UT’s Department of Materials Science and Engineering. Since then, his research 
has focused on making new, high-value materials from renewable, plant-based 
sources. Dr. Harper can be contacted by email: 
dharp...@utk.edu .





==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e lifesciences@bnl.gov

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973






To unsubscribe from the CCP4BB list, click the following link:
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[ccp4bb] CBMS Lecture Series - "Engineered Carbon Materials Derived from Lignin for Energy Storage" - November 16, 13:30

[Stojanoff, Vivian]

You are cordially invited to join  the Center for Biomolecular Structure 
Lecture Series ………..



David P. Harper

Center for Renewable Carbon, The University of Tennessee

WEDNESDAY, November 16, 13:30 (EST)



"Engineered Carbon Materials Derived from Lignin for Energy Storage"



Register in advance for this meeting:
  https://bnl.zoomgov.com/meeting/register/vJIsf-GuqjkvHvUBsoAXXwWoAjcRqXR8BPA​​



  Time conversion Link: 
https://www.worldtimebuddy.com/



Abstract:

Lignin’s carbon-dense aromatic structure and abundance promise to replace 
carbon derived from fossil or mined sources. However, lignin’s heterogeneous, 
amorphous structure and difficulty isolating it in high purity from woody 
feedstocks make predicting processing performance and carbon structure 
difficult. Strategies for processing multiple lignin feedstocks from 
organosolv, kraft, and other fractionation technologies into carbon materials, 
along with the relative advantages/disadvantages of carbon from traditional 
sources. Further, the influence of processing and lignin sources on the 
development of carbon structure will be addressed. Preliminary models for 
lignin-based carbon materials will be presented along with potential 
implications for their use in energy storage and beyond.



Bio:

Dr. Harper earned a BA in Physics from West Virginia University and a Ph.D. in 
Civil Engineering from Washington State University in 2003, focusing on 
structural composite materials. He was a Post-Doctoral Fellow at the USDA 
Forest Products Laboratory in Madison, WI. Dr. Harper joined the Department of 
Forestry, Wildlife, and Fisheries in 2004 at the University of Tennessee 
located within UT’s Institute of Agriculture and is a joint faculty member in 
UT’s Department of Materials Science and Engineering. Since then, his research 
has focused on making new, high-value materials from renewable, plant-based 
sources. Dr. Harper can be contacted by email: 
dharp...@utk.edu .





==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e lifesciences@bnl.gov

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973






To unsubscribe from the CCP4BB list, click the following link:
https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB=1

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[ccp4bb] CBMS Lecture Series - November 16

[Stojanoff, Vivian]

You are cordially invited to join  the Center for Biomolecular Structure 
Lecture Series ………..





David P. Harper

Center for Renewable Carbon, The University of Tennessee



WEDNESDAY, November 16, 13:30 (EST)



"Engineered Carbon Materials Derived from Lignin for Energy Storage"



Register in advance for this meeting:

  https://bnl.zoomgov.com/meeting/register/vJIsf-GuqjkvHvUBsoAXXwWoAjcRqXR8BPA​​



  Time conversion Link: 
https://www.worldtimebuddy.com/



Abstract:

Lignin’s carbon-dense aromatic structure and abundance promise to replace 
carbon derived from fossil or mined sources. However, lignin’s heterogeneous, 
amorphous structure and difficulty isolating it in high purity from woody 
feedstocks make predicting processing performance and carbon structure 
difficult. Strategies for processing multiple lignin feedstocks from 
organosolv, kraft, and other fractionation technologies into carbon materials, 
along with the relative advantages/disadvantages of carbon from traditional 
sources. Further, the influence of processing and lignin sources on the 
development of carbon structure will be addressed. Preliminary models for 
lignin-based carbon materials will be presented along with potential 
implications for their use in energy storage and beyond.



Bio: Dr. Harper earned a BA in Physics from West Virginia University and a 
Ph.D. in Civil Engineering from Washington State University in 2003, focusing 
on structural composite materials. He was a Post-Doctoral Fellow at the USDA 
Forest Products Laboratory in Madison, WI. Dr. Harper joined the Department of 
Forestry, Wildlife, and Fisheries in 2004 at the University of Tennessee 
located within UT’s Institute of Agriculture and is a joint faculty member in 
UT’s Department of Materials Science and Engineering. Since then, his research 
has focused on making new, high-value materials from renewable, plant-based 
sources. Dr. Harper can be contacted by email: dharp...@utk.edu .




==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e lifesciences@bnl.gov

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973



Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.








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[ccp4bb] Reminder: CBMS Structural Biology Workbench

[Stojanoff, Vivian]

Dear Colleagues,

We'd like to bring to your attention that the registration is open for the CBMS 
Structural Biology Workbench, scheduled September 27 through 29. Participants 
can choose between SAXS and MX or attend both. The event will be held 
virtually.  Registration is free:

https://www.bnl.gov/cbmsworkbench/

Any questions can be directed to Vivian Stojanoff (stoja...@bnl.gov).

Kind regards,

Vivian

--
Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
p 1(631) 344 8375
e nsls.lifescien...@gmail.com
w https://www.bnl.gov/ps/lifesciences/

Address:
Center for Biomolecular Structure
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973

Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.





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[ccp4bb] CBMS Structural Biology Workbench September 27 to 29 - Registration open

[Stojanoff, Vivian]

Dear Colleagues,

We'd like to bring to your attention that the registration is open for the CBMS 
Structural Biology Workbench, scheduled September 27 through 29. Participants 
can choose between SAXS and MX or attend both. The event will be held 
virtually.  Registration is free:

https://www.bnl.gov/cbmsworkbench/

Participants are encouraged to send samples. Registration Deadline for sending 
samples August 26 2022. Please contact James Byrnes (byr...@bnl.gov) if sending 
SAXS samples or Vivian Stojanoff (stoja...@bnl.gov) if sending samples for MX.

Kind regards,

Vivian

--
Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
p 1(631) 344 8375
e nsls.lifescien...@gmail.com
w https://www.bnl.gov/ps/lifesciences/

Address:
Center for Biomolecular Structure
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973

Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.





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https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB=1

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hosted by www.jiscmail.ac.uk, terms & conditions are available at 
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[ccp4bb] CBMS Lecture Series - June 15, 2022; 13:30 - Andrea Markelz - University of Buffalo

[Stojanoff, Vivian]

Please join us for ……



Andrea Markelz

University of Buffalo, SUNY



WEDNESDAY, June 15, 13:30 (EDT)



"Uncovering Protein Structural Dynamics with Terahertz Light"



Register in advance for this meeting:

https://bnl.zoomgov.com/meeting/register/vJItcOqurTssEgjFKexuOYLrWgcG4CkJUKo



Time conversion Link: 
https://www.worldtimebuddy.com/



Abstract:

The long-range structural vibrations of biomacromolecules (molecular weight > 
5kDa), are matched to biological thermal energies.  This intriguing overlap 
raises the question if, like sequence and structure, these dynamics are also 
evolutionarily optimized for robust and efficient biochemistry.  The vibrations 
for such massive systems are necessarily complex.  The structural vibrations 
involve displacements of entire subdomains, are numerous and closely spaced in 
energy, leading to dense spectra.  The spectra are further complicated by the 
energy overlap with collective excitations of the biological water necessary 
for in vivo structure and biological relevance.  Compounded with these effects, 
while a single spectrum corresponds to a single structure, biomacromolecular 
structure thermally samples small configurational changes in time, leading to 
variation in the vibrational spectra.  These effects all lead to the smooth 
featureless spectra seen by investigators for macroscopic samples. In this talk 
I will provide an overview of terahertz biomolecular studies and discuss the 
fundamental issue of isolating vibrational excitations based on specific 
structural displacements.  An example of a technique to provides this isolation 
is anisotropic terahertz microspectroscopy (ATM).  Using ATM we have found that 
indeed there are biases in the directionality of vibrational displacements 
which change with ligand binding and photoexcitation.  In particular 
photoexcitation measurements of orange carotenoid protein (OCP) demonstrate 
that intermediate states of the photo cycle coincide with changes in the 
directionality of vibrations, suggesting these reorganizations of the dynamics 
may assist with access to intermediate state structures.  Finally, I will 
discuss the challenges of current instrumentation, computational tools and 
sample preparation that need to be addressed to more fully realize the 
potential of THz in the understanding of the role of picosecond structural 
dynamics in biology.



















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[ccp4bb] CBMS Workbench - Structural Biology June 6-8 2022

[Stojanoff, Vivian]

Dear Colleagues

We'd like to bring to your attention that registration is open for the CBMS 
Structural Biology  workbenches scheduled June 6 through 8. Participants can 
choose between Solution Scattering and MX or attend both. Intended as an 
information and training for new members and refresher for those experienced 
members the Workbench invites participants to send their samples and measure 
them during the workbenches.

Register for free:

https://www.bnl.gov/cbmsworkbench/

Registration deadlines:

May 23, 2022 if  sending samples
June 1st , 2022 if  attending lectures, tutorials and demonstrations

Those sending samples should also contact Vivian Stojanoff (stoja...@bnl.gov) 
and James Byrnes (jbyr...@bnl.gov) or phone (631) 344 8375;  for more 
information.

Kind regards,

Vivian

==

Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p: 1(631) 344 8375

e: nsls.lifescien...@gmail.com 

https://www.bnl.gov/nsls2/lifesciences/


Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973


*Supporting Grants:*CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BESunder 
contract # DE-SC0012704.




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hosted by www.jiscmail.ac.uk, terms & conditions are available at 
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[ccp4bb] Reminder: CBMS Lecture Series - May 18, 2022; 13:30 - Michael Ragusa, Dartmouth College

[Stojanoff, Vivian]

Please join us for ……



Michael Ragusa

Dartmouth College



WEDNESDAY, May 18, 13:30 (EDT)



"Two Stories of Degradation – Investigating the Initiation of Selective 
Autophagy in Yeast"



Register in advance for this meeting:


 https://bnl.zoomgov.com/meeting/register/vJIsde6ppjIqGCTAbMCARjdtKas5xKciYEg



San Francisco 10:30 - NYC 13:30 -  London 18:30 - Paris 19:30 - Mumbai 23:00 - 
Tokio 2:30 (May 19) - Sidney 3:30 (May 19)



Abstract:

Autophagy is a cellular degradation process in which cytosolic material is 
captured in double membrane vesicles and targeted to lysosomes in mammalian 
cells or the vacuole in yeast for degradation. One cargo that can be degraded 
by autophagy is mitochondria. The degradation of mitochondria by autophagy 
requires the organization of many soluble proteins on the surface of 
mitochondria to generate distinct initiation sites for this process. We have 
been utilizing a combination of biochemistry, cell biology and structural 
biology to investigate how these initiation sites are organized and how these 
initiation sites recruit membrane.





[cid:4bbce247-f69d-4c92-837f-5dabeb00c441]



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DTSTART;TZID=America/New_York:20220518T133000
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SUMMARY:CBMS Lecture Series - Michael Ragusa
UID:20220511T183414Z-1612718902@fe80:0:0:0:4f3:3aff:fe13:dd60eth0
TZID:America/New_York
DESCRIPTION:Vivian Stojanoff is inviting you to a scheduled ZoomGov meeti
 ng.\n\nJoin ZoomGov Meeting\nhttps://bnl.zoomgov.com/j/1612718902?pwd=Z3
 I0d3FkNU43c0huc1RTVkZjSklvUT09\n\nMeeting ID: 161 271 8902\nPasscode: 30
 1056\nOne tap mobile\n+16692545252\,\,1612718902#\,\,\,\,*301056# US (Sa
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 al by your location\n+1 669 254 5252 US (San Jose)\n+1 6
 46 828 7666 US (New York)\n+1 551 285 1373 US\n+1 669 21
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[ccp4bb] CBMS Lecture Series - May 18, 2022, 13:30 (EDT) - Michael Ragusa

[Stojanoff, Vivian]

[cid:8d57e64b-4fa9-4d05-be2a-f682e67af459]



Please join us for ……



Michael Ragusa

Dartmouth College



WEDNESDAY, May 18, 13:30 (EDT)



"Two Stories of Degradation – Investigating the Initiation of Selective 
Autophagy in Yeast"



Register in advance for this meeting:


 https://bnl.zoomgov.com/meeting/register/vJIsde6ppjIqGCTAbMCARjdtKas5xKciYEg



San Francisco 10:30 - NYC 13:30 -  London 18:30 - Paris 19:30 - Mumbai 23:00 - 
Tokio 2:30 (May 19) - Sidney 3:30 (May 19)



Abstract:

Autophagy is a cellular degradation process in which cytosolic material is 
captured in double membrane vesicles and targeted to lysosomes in mammalian 
cells or the vacuole in yeast for degradation. One cargo that can be degraded 
by autophagy is mitochondria. The degradation of mitochondria by autophagy 
requires the organization of many soluble proteins on the surface of 
mitochondria to generate distinct initiation sites for this process. We have 
been utilizing a combination of biochemistry, cell biology and structural 
biology to investigate how these initiation sites are organized and how these 
initiation sites recruit membrane.



On behalf of Vivian Stojanoff,

Linda J. Hanlon

Executive Assistant to Dr. James Misewich

Associate Laboratory Director for Energy and Photon Sciences

Brookhaven National Laboratory

Building 460

Upton, NY  11973-5000

Office:  (631) 344-7517

han...@bnl.gov

[cid:3d332d44-3bfb-44f7-950b-69ceb7cba57a]




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DTSTART:19701101T02
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END:STANDARD
END:VTIMEZONE
BEGIN:VEVENT
DTSTAMP:20220511T183414Z
DTSTART;TZID=America/New_York:20220518T133000
DTEND;TZID=America/New_York:20220518T143000
SUMMARY:CBMS Lecture Series - Michael Ragusa
UID:20220511T183414Z-1612718902@fe80:0:0:0:4f3:3aff:fe13:dd60eth0
TZID:America/New_York
DESCRIPTION:Vivian Stojanoff is inviting you to a scheduled ZoomGov meeti
 ng.\n\nJoin ZoomGov Meeting\nhttps://bnl.zoomgov.com/j/1612718902?pwd=Z3
 I0d3FkNU43c0huc1RTVkZjSklvUT09\n\nMeeting ID: 161 271 8902\nPasscode: 30
 1056\nOne tap mobile\n+16692545252\,\,1612718902#\,\,\,\,*301056# US (Sa
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 al by your location\n+1 669 254 5252 US (San Jose)\n+1 6
 46 828 7666 US (New York)\n+1 551 285 1373 US\n+1 669 21
 6 1590 US (San Jose)\nMeeting ID: 161 271 8902\nPasscode: 301056\nFind y
 our local number: https://bnl.zoomgov.com/u/amCUHaV9l\n\nJoin by SIP\n16
 12718...@sip.zoomgov.com\n\nJoin by H.323\n161.199.138.10 (US West)\n161
 .199.136.10 (US East)\nMeeting ID: 161 271 8902\nPasscode: 301056\n\n
LOCATION:https://bnl.zoomgov.com/j/1612718902?pwd=Z3I0d3FkNU43c0huc1RTVkZ
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[ccp4bb] CBMS Structural Biology Workbench - SAXS & MX - June 6 -8, 2022

[Stojanoff, Vivian]

Dear Colleagues

We'd like to bring to your attention that registration is open for the CBMS 
Structural Biology workbenches - SAXS & MX- scheduled June 6 through 8. 
Participants can choose between Solution Scattering and MX or attend both.  
Participants are  invited to send samples and measure them during the 
workbenches.

Register for free:

https://www.bnl.gov/cbmsworkbench/

Registration deadlines:

May 23, 2022 if  sending samples for practical session
June 1st , 2022 if  attending only lectures, tutorials and demonstrations

Those sending samples should also contact Vivian Stojanoff (stoja...@bnl.gov) 
and James Byrnes (jbyr...@bnl.gov)  for more information.

Kind regards,

Vivian

-- -
Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
p 1(631) 344 8375
e lifescie...@bnl.gov
w 
https://www.bnl.gov/ps/lifesciences/

Address:
Center for Biomolecular Structure
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973

Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.








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[ccp4bb] Reminder: CBMS Lecture Series - Dr Sibel Yalcin - March 16, 13:30, DST

[Stojanoff, Vivian]

Please join us……



Sidel Yalcin

Yale University



WEDNESDAY, MARCH 16, 13:30 (DST)



"Electrogenetic Control of Bacteria via Protein Nanowires Capable of Ultrafast 
Charge Transport and

Storage for Next-Generation of Bioelectronic Materials and Devices"



Register in advance for this meeting:

  https://bnl.zoomgov.com/meeting/register/vJItc-yvpzsoHF1vnGho1CztnA-wRfHzxI4



Abstract:

Commercial bioelectronic devices to date rely on silicon-based technology. 
Despite decades of effort, current structural, electronic, and optical 
materials remain fundamentally bioincompatible. Synthetic conducting polymers 
are typically stiff and brittle, as well as non-biodegradable, and show poor 
stability and performance due to disorder. We aim to leverage the unique 
ability of bacterial systems to synthesize electronic materials with high 
conductivity and ability to self-repair and replicate. Electrogenetics has 
potential to efficiently control bacterial growth, adhesion, and communication. 
We have found that electric fields can directly control bacterial synthesis of 
nanowires made up of cytochromes OmcS (Cell 2019) and OmcZ (Nature Chem.Bio. 
2020) without any mediators. We have further found that the nanowires are 
translocated to the bacterial surface using pili that serve as a piston to 
secrete cytochromes rather than functioning as nanowires as previously thought.



World Clock: NYC (DST)  13:30;  London 17:30; Paris 18:30; New Delhi 11:00 PM; 
Shanghai 1:30 AM (Thursday); Tokio 2:30 AM (Thursday); Sidney  4:30 am 
Thursday; San Francisco 10:30 AM (PCT)




==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e nsls.lifescien...@gmail.com

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973







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[ccp4bb] CBMS Lecture Series - Dr Sibel Yalcin - March 16, 13:30, DST

[Stojanoff, Vivian]

Please join us……



Sidel Yalcin

Yale University



WEDNESDAY, MARCH 16, 13:30 (DST)



"Electrogenetic Control of Bacteria via Protein Nanowires Capable of Ultrafast 
Charge Transport and

Storage for Next-Generation of Bioelectronic Materials and Devices"



Register in advance for this meeting:

  https://bnl.zoomgov.com/meeting/register/vJItc-yvpzsoHF1vnGho1CztnA-wRfHzxI4



Abstract:

Commercial bioelectronic devices to date rely on silicon-based technology. 
Despite decades of effort, current structural, electronic, and optical 
materials remain fundamentally bioincompatible. Synthetic conducting polymers 
are typically stiff and brittle, as well as non-biodegradable, and show poor 
stability and performance due to disorder. We aim to leverage the unique 
ability of bacterial systems to synthesize electronic materials with high 
conductivity and ability to self-repair and replicate. Electrogenetics has 
potential to efficiently control bacterial growth, adhesion, and communication. 
We have found that electric fields can directly control bacterial synthesis of 
nanowires made up of cytochromes OmcS (Cell 2019) and OmcZ (Nature Chem.Bio. 
2020) without any mediators. We have further found that the nanowires are 
translocated to the bacterial surface using pili that serve as a piston to 
secrete cytochromes rather than functioning as nanowires as previously thought.



World Clock: NYC (DST)  13:30;  London 17:30; Paris 18:30; New Delhi 11:00 PM; 
Shanghai 1:30 AM (Thursday); Tokio 2:30 AM (Thursday); Sidney  4:30 am 
Thursday; San Francisco 10:30 AM (PCT)




==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e nsls.lifescien...@gmail.com

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973







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[ccp4bb] Reminder: CBMS Lecture Series: Wednesday February 16, 13:30 pm (NY time zone)

[Stojanoff, Vivian]

You are cordially invited to join  the Center for Biomolecular Structure 
Lecture Series ………..





Jochen Hub

Universität des Saarlandes



WEDNESDAY, February 16, 13:30 (EST)





"Structure and ensemble refinement against SWAXS data with explicit-solvent MD 
simulations"



Register in advance for this meeting:



 https://bnl.zoomgov.com/meeting/register/vJItc-yvqj4uG9ryjG2Se_JF3fZh5MJQgQc



Abstract:

Small-angle and wide-angle X-ray scattering in solution (SAXS, WAXS, SWAXS) is 
an increasingly accurate method for obtaining structural information on 
biomolecules and soft-matter complexes in solution. However, the interpretation 
of the solution scattering data by computational methods is complicated by (i) 
the low information content of the data and (ii) by scattering contributions 
from the hydration layer and excluded solvent, leading to a significant risk of 
over interpretation upon fitting structural models against SWAXS data.To 
overcome such problems, we have developed methods for interpreting SWAXS data 
with all-atom explicit-solvent molecular dynamics (MD) simulations. In this 
talk we show how  MD simulations aid the interpretation of SWAXS data in 
multiple manners: The physical information in atomistic force fields 
complements the low information SWAXS data; explicit-solvent MD is used to 
predict solvent scattering contributions, and the MD-related sampling methods 
may guide the structure refinement against SWAXS data.



==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e nsls.lifescien...@gmail.com

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973




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[ccp4bb] CBMS Lecture Series - February 16, 2022 - 13:30 New York time zone

[Stojanoff, Vivian]

You are cordially invited to join  the Center for Biomolecular Structure 
Lecture Series ………..





Jochen Hub

Universität des Saarlandes



WEDNESDAY, February 16, 13:30 (EST)





"Structure and ensemble refinement against SWAXS data with explicit-solvent MD 
simulations"



Register in advance for this meeting:


 https://bnl.zoomgov.com/meeting/register/vJItc-yvqj4uG9ryjG2Se_JF3fZh5MJQgQc



Abstract:

Small-angle and wide-angle X-ray scattering in solution (SAXS, WAXS, SWAXS) is 
an increasingly accurate method for obtaining structural information on 
biomolecules and soft-matter complexes in solution. However, the interpretation 
of the solution scattering data by computational methods is complicated by (i) 
the low information content of the data and (ii) by scattering contributions 
from the hydration layer and excluded solvent, leading to a significant risk of 
over interpretation upon fitting structural models against SWAXS data.To 
overcome such problems, we have developed methods for interpreting SWAXS data 
with all-atom explicit-solvent molecular dynamics (MD) simulations. In this 
talk we show how  MD simulations aid the interpretation of SWAXS data in 
multiple manners: The physical information in atomistic force fields 
complements the low information SWAXS data; explicit-solvent MD is used to 
predict solvent scattering contributions, and the MD-related sampling methods 
may guide the structure refinement against SWAXS data.


==



Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e nsls.lifescien...@gmail.com

w https://www.bnl.gov/ps/lifesciences/



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973




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[ccp4bb] CBMS workbenches - Structural Biology

[Stojanoff, Vivian]

Dear All,

You are cordially invited to participate in the Center for Biomolecular 
Structure workbenches on solution scattering and macromolecular 
crystallography.  Choose between workbenches or select both and learn of 
alternative structure determination methods. To register for the February 2 
through 4, 2021 session follow instructions through the link bellow. 
Registration is free and open to the public

https://www.bnl.gov/cbmsworkbench/


Those participants who chose to send samples to study during the workbench 
should contact organizers and register by January 15.  Data collection session 
and analysis will be shared.

Happy New Year!

Vivian
​
===
Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
p 1(631) 344 8375
e nsls.lifescien...@gmail.com
w https://www.bnl.gov/ps/lifesciences/

Address:
Center for Biomolecular Structure
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973

Supporting Grants: CBMS is supported by NIH-NIGMS #P30GM133893, and by the 
DOE-BER #KP1605010. Any work performed at NSLS-II is supported by DOE-BES  
under contract # DE-SC0012704.




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[ccp4bb] Reminder: CBMS Lecture Series - October 20 - Lee Makowski

[Stojanoff, Vivian]

Please join us ………..



Molecular Events in the Progression of Alzheimer’s Disease



Lee Makowski



Northeastern University



WEDNESDAY, October 20, 13:30 (EST)



Register in advance for this meeting:

https://bnl.zoomgov.com/meeting/register/vJIscuqgrD0vG8SVmZ49QwTrS8eGSZrs-1U



Abstract:

Fibrillar aggregates of Abeta peptides and tau protein are defining features of 
Alzheimer's disease (AD) but the role these structures play in the etiology of 
disease remains uncertain. Outstanding questions remain as to the distribution 
of polymorphs between and within cases.  We are using x-ray scanning 
microdiffraction on histological sections of human brain tissue in order to map 
the distribution and arrangement of fibrillar aggregates of these proteins in 
plaques and tangles.  The central hypothesis of the work is that the spatial 
distribution of structural polymorphs in brain tissue will provide important 
clues as to how fibrils contribute to disease.  Our goals are to assess whether 
or not different fibrillar polymorphs spread by a prion-like process during 
disease progression and to produce data that will provide insight into the 
structural basis by which different fibrillar strains are associated with 
different disease subtypes.






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[ccp4bb] Reminder: CBMS Workbench - October 11-13, 2021 - SAXS and MX

[Stojanoff, Vivian]

Dear All,

You are cordially invited to participate in the Center for Biomolecular 
Structure workbenches on solution scattering and macromolecular 
crystallography.  Registration is open for the October 11 through 13, 2021 
session and is free.

https://www.bnl.gov/cbmsworkbench/

Choose between workbenches or select both and learn of alternative structure 
determination methods. Participants will have the opportunity to send samples 
to measure during the workbench. Data analysis will be shared. If you are 
planning to send samples, make sure to register early to obtain the necessary 
credentials for remote access to the beam lines.

Invited Speakers:

Tutorials and Talks

- Elspeth Garman (University of Oxford)  - Radiation Damage: what is it and how 
can it be minimized?
To gain the most from the tutorial and to run the software yourselves, 
attendees should upload the new RADDOSE-3D GUI from the Garman group github 
site. Instructions will be made available to those interested
- Al Kikhney (Xenocs Nordic ApS.)   - Ensemble Optimization Method (EOM) - 
SAXS-based modeling of flexible and disordered proteins
- Kay Diederichs (Universitaet Konstanz)   - Data processing using XDS, and 
data quality assessment
Kay invites Participants with interesting data sets should contact Kay, 
kay.diederi...@uni-konstanz.de, prior to 
the workshop.
- Dorothee  Liebschner (Berkeley Lab)  - Using Phenix for crystallographic data

- Vukica Srajer (University of Chicago) -  Protein Dynamics: Time-resolved 
Macromolecular Crystallography


Panel Discussion - Difficult structures


- Maria Bewley (Penn State)
- Kevin Battaile (NY Structural Biology Center)
- Sean McSweeney (Center for Biomolecular Structure, BNL)

To register follow the link:
https://www.bnl.gov/cbmsworkbench/

Registration is a two-step process if you are not a BNL guest. If you have a 
BNL guest appointment you need only to register for the workbenches.

Kind regards

Vivian




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[ccp4bb] CBMS WORKBENCH - SAXS and MX - October 11 - 13, 2021

[Stojanoff, Vivian]

Dear All,

You are cordially invited to participate in the Center for Biomolecular 
Structure workbenches on solution scattering and macromolecular 
crystallography. Registration is open for the October 11 through 13, 2021 
session and is free.

https://www.bnl.gov/cbmsworkbench/

Choose between workbenches or select both and learn of alternative structure 
determination methods. Participants will have the opportunity to send samples 
to measure during the workbench. Data analysis will be shared. If you are 
planning to send samples, make sure to register early to obtain the necessary 
credentials for remote access to the beam lines.


Invited Speakers:

- Elspeth Garman (University of Oxford)
- Al Kikhney (Xenocs Nordic ApS.)
- Kay Diederichs (Universitaet Konstanz)
- Dorothee  Liebschner (Berkeley Lab)
- Vukica Srajer (University of Chicago
- Maria Bewley (Penn State)
- Kevin Battaile (NY Structural Biology Center)
- Sean McSweeney (Center for Biomolecular Structure, BNL)

To register follow the link:

https://www.bnl.gov/cbmsworkbench/

Registration is a two-step process if you are not a BNL guest. If you have a 
BNL guest appointment you need only to register for the workbenches.

Kind regards

Vivian

--
Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
p 1(631) 344 8375
e nsls.lifescien...@gmail.com
w https://www.bnl.gov/ps/lifesciences/

Address:
Center for Biomolecular Structure
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973




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https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB=1

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hosted by www.jiscmail.ac.uk, terms & conditions are available at 
https://www.jiscmail.ac.uk/policyandsecurity/

[ccp4bb] CBMS Workbench - SAXS & MX - October 11 t0 13, 2021

[Stojanoff, Vivian]

Dear All,

You are cordially invited to participate in the Center for Biomolecular 
Structure workbenches on solution scattering and macromolecular 
crystallography. Registration is open for the October 11 through 13, 2021 
session and is free.

https://www.bnl.gov/cbmsworkbench/

Choose between workbenches or select both and learn of alternative structure 
determination methods. Participants will have the opportunity to send samples 
to measure during the workbench. Data analysis will be shared. If you are 
planning to send samples, make sure to register early to obtain the necessary 
credentials for remote access to the beam lines.


Invited Speakers:

- Elspeth Garman (University of Oxford)
- Al Kikhney (Xenocs Nordic ApS.)
- Kay Diederichs (Universitaet Konstanz)
- Dorothee  Liebschner (Berkeley Lab)

To register follow the link:

https://www.bnl.gov/cbmsworkbench/

Registration is a two-step process if you are not a BNL guest. If you have a 
BNL guest appointment you need only to register for the workbenches.

Kind regards

Vivian

--
Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
p 1(631) 344 8375
e nsls.lifescien...@gmail.com
w https://www.bnl.gov/ps/lifesciences/

Address:
Center for Biomolecular Structure
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973




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[ccp4bb] CBMS Lecture Series - 22 September 2021 - Chris Brosey

[Stojanoff, Vivian]

Please join us ………..


Center for Biomolecular Structure Lecture Series



Incorporating HT-SAXS into Structure-Driven Drug Discovery Pipelines


Chris Brosey


M.D. Anderson Cancer Center, The University of Texas


WEDNESDAY, September 22, 13:30 (EST - NY time zone)



Register in advance for this meeting:

   https://bnl.zoomgov.com/meeting/register/vJIsfu6przwpH8NymLh_TKxtg09_NaMkFFs



Abstract:

High-throughput (HT) methods for discovering single-target protein and nucleic 
acid ligands are well established and routinely utilized for drug discovery. 
Many critical biological outcomes, however, are mediated by multi-component 
assemblies and dynamic macromolecular architectures. HT approaches to assess 
and fine-tune ligand impact on such functional, dynamic systems remain 
underdeveloped. Small-angle X-ray scattering (SAXS) provides an opportunity to 
monitor changes to biomolecular architectures and assemblies under native 
solution environments, enabling chemical screening and selection for specific 
architectural states. I will discuss how we have incorporated time-resolved 
HT-SAXS into a classic fragment screening pipeline and used this approach to 
identify chemical allosteric effectors targeting functional architectures of 
mitochondrial Apoptosis-Inducing Factor (AIF)

---
Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
p 1(631) 344 8375
e nsls.lifescien...@gmail.com
w https://www.bnl.gov/ps/lifesciences/

Address:
Center for Biomolecular Structure
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973




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[ccp4bb] Reminder - CBMS Lecture Series - Mark Chance - Using protein footprinting .....

[Stojanoff, Vivian]

Please join us………..



Using protein footprinting to make structural biology easier: Case studies from 
academia and industry

Mark R. Chance

Vice Dean for Research, School of Medicine

School of Medicine

Case Western Reserve University



TUESDAY August 24, 2021, 13:30 (EDT)



Register in advance for this meeting:

 https://bnl.zoomgov.com/meeting/register/vJIsc-ihrzojGWhKFsUxX-wcU3RgxNgEZ6k






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[ccp4bb] CBMS Lecture Series - Mark Chance - August 24, 2021

[Stojanoff, Vivian]

Please join us………..



Using protein footprinting to make structural biology easier: Case studies from 
academia and industry

Mark R. Chance

Vice Dean for Research

School of Medicine

Case Western Reserve University



TUESDAY August 24, 2021, 13:30 (EDT)



Register in advance for this meeting:

 https://bnl.zoomgov.com/meeting/register/vJIsc-ihrzojGWhKFsUxX-wcU3RgxNgEZ6k



Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
Center for Biomolecular Structure
National Synchrotron Light Source II
Brookhaven National Laboratory
p 1(631) 344 8375
e nsls.lifescien...@gmail.com
w https://www.bnl.gov/nsls2/lifesciences/




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[ccp4bb] CBMS Lecture Series - July 14, 2021

[Stojanoff, Vivian]

Dear Colleagues

You are cordially invited to attend the virtual CBMS Lecture Series .


An outlook on cryo-electron microscopy for structural and cellular biology



Raimond Ravelli

Associate Professor

Institute of Nanoscopy (IoN), M4I,

Fac. Health, Medicine and Life Sciences

Maastricht University



July 14, 2021, 13:30 (EDT)



Register in advance for this meeting:
https://bnl.zoomgov.com/meeting/register/vJIsdOCopzouHUg5FoLj2CPuhFjhAZo8yis

Abstract

Cryo-EM has become a powerful tool for structural and cellular biologists to 
study the structure-function relationships of their biomolecules of interest. 
Recent development of TEM hardware has led to atomic resolution for single 
particle cryo-EM, and near-atomic resolution for macromolecular complexes 
within cells. Most of the current successes have been reached using 
conventional phase contrast cryo-TEM. In this talk, I will discuss current 
limitations in cryo-EM such as sample preparation and detectors and show some 
of the developments therein. Could it become possible to solve a structure, as 
small as hen egg white lysozyme, by single particle cryo-EM? We will review 
alternative, exotic cryo-EM methods, with different information transfer 
functions. These include TEM techniques such as phase plate, multi-pass TEM, 
and off-axis holography, as well as STEM techniques, such as ptychography, and 
a quantum sorter.

Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
Center for Biomolecular Structure
National Synchrotron Light Source II
Brookhaven National Laboratory
p 1(631) 344 8375
e nsls.lifescien...@gmail.com
w https://www.bnl.gov/nsls2/lifesciences/





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[ccp4bb] Invitation CBMS Lecture Series - June 16, 2021, 13:30 (EDT)

[Stojanoff, Vivian]

Dear CCP4 colleagues,

You are cordially invited to the Center for Biomolecular Structure (virtual) 
lecture series,



An odyssey in drug delivery study via X-ray microscopy approach



Dr. Yang Yang

National Synchrotron Light Source II



June 16, 2021, 13:30 (EDT)



Registration Link:

https://bnl.zoomgov.com/meeting/register/vJItfuuurzsjG-VF9klmmilw7nbOH8Qcy5s





Abstract

We’ve used X-ray fluorescence microscopy (XRF) as a powerful chemical 
nano-imaging tool to study a few examples of anti-cancer drug with transition 
metal complexes (Os, Ir) and locate their target sites within human cancer 
cells. Throughout these studies, despite its high sensitivity, 
semi-quantitative, and versatility, XRF has also complemented other techniques 
such as soft X-ray microscopy, TEM, cryo light confocal microscopy, and hard 
X-ray phase contrast imaging to provide more complete pictures to uncover the 
potential delivery mechanisms. In addition, sample preparations including 
cryogenic preparation, as well as the transfer compatibility between various 
techniques, as a critical aspect, will also be discussed.

The CBMS Team

---
Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
p 1(631) 344 8375
e nsls.lifescien...@gmail.com
w https://www.bnl.gov/nsls2/lifesciences/

Address:
Center for Biomolecular Structure
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973




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[ccp4bb] Center for Biomolecular Structure Lecture Series

[Stojanoff, Vivian]

Dear CCP4 researchers,

You are cordially invited to the Center for Biomolecular Structure (virtual) 
lecture series,



Structure Function of Lipid Metabolism



Dr. Michael Airola

Stony Brook University



May 26, 2021, 13:30 (EST)



Registration Link:
https://bnl.zoomgov.com/meeting/register/vJIsfu2rpjwoHo4pf6YNKlcfy8i8LOUBOsg





Abstract

Lipids not only form the basis of our cell membranes but also serve as 
bioactive signaling molecules that regulate critical cellular and pathological 
processes. The enzymes that generate and breakdown these bioactive lipids have 
emerged as therapeutic targets for treating the leading causes of diseases 
including cancer, cardiovascular disease, and diabetes. As a promising 
pharmaceutical target, we will review the role of these lipids metabolizing 
enzymes at the molecular and structural level.

The CBMS Team

---
Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
p 1(631) 344 8375
e nsls.lifescien...@gmail.com
w https://www.bnl.gov/nsls2/lifesciences/

Address:
Center for Biomolecular Structure
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973




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[ccp4bb] The CBMS SAXS and MX workbenches

[Stojanoff, Vivian]

Dear Colleagues,

The Center for Biomolecular Structure (CBMS), at the National Synchrotron Light 
Source II,  invites you to participate in the BioMolecular Solution Scattering 
(SAXS/WAXS) and Macromolecular Crystallography (MX) workbenches.  Scheduled 
back-to-back, June 7 through 9, these virtual training workshops are aimed at 
researchers that would like to know more about forefront techniques and methods 
available at the CBMS structural biology beamlines.  Participants are 
encouraged to register for both workshops (https://www.bnl.gov/cbmsworkbench/). 
 If you would like to analyze your sample(s) as part of the workshop,  contact 
James Byrnes (jbyr...@bnl.gov) for SAXS/WAXS and Vivian Stojanoff 
(stoja...@bnl.gov) for MX samples no later than May 28, 2021.

Registration is FREE!  Early registration closes May 24;  Registration closes 
May 28.

https://www.bnl.gov/cbmsworkbench/
Center for BioMolecular Structure 
Workbenches
Scope. The BioMolecular Solution Scattering (SAXS/WAXS) and Macromolecular 
Crystallography (MX) workbenches span three days of virtual training classes 
aimed at researchers that would like to know more about forefront techniques 
and methods available to scientists at BNL’s Center for Biomolecular Structure 
(CBMS) structural biology beamlines.
www.bnl.gov


Kind regards,

The CBMS Team
-
Center for Biomolecular Structure
https://www.bnl.gov/nsls2/lifesciences/
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973




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[ccp4bb] CBMS Lecture Series, Wednesday April 21st, 13:30 (EST)

[Stojanoff, Vivian]

You are cordially invited to the Center for Biomolecular Structure Lecture 
Series,



Lanthanide-Binding Tags for 3D X-Ray Imaging of Proteins in Cells at Nanoscale 
Resolution



Lisa Miller, NSLS II Brookhaven National Laboratory

April 21, 2021, 13:30 (EST - NY time zone)

Link:  
https://bnl.zoomgov.com/meeting/register/vJItde2vrzotEhRC0VBwCs8cLqfFNJV3M3c





Abstract

X-ray Fluorescence Microscopy (XFM) is a powerful method for imaging the 
trace-element concentration, distribution, and speciation in cells and tissues. 
Even though the technique has been around for more than 30 years, only recently 
have advances in X-ray sources, optics, and detectors enabled two- and 
three-dimensional X-ray imaging at the nanoscale with attogram detection 
sensitivity. However, one limitation of XFM for imaging biological systems is 
detecting the trace-element distribution in the context of subcellular 
organelles and individual proteins. For visible light microscopy, the most 
ubiquitous method for imaging individual proteins within the context of a 
living cell is the use of intrinsically fluorescent proteins, such as the green 
fluorescent protein (GFP) that is co-expressed as a fusion tag along with the 
protein of interest.  However, visualization of these tags is limited by the 
wavelengths of visible light except by applying specialized super resolution 
approaches.  Here, we are developing applications enabled by encoded 
lanthanide-binding tags (LBTs), which are GFP-like analogs of minimal size (ca. 
15-20 amino acids) for XFM. In this talk, applications of LBTs to both 
membrane-bound and cytosolic proteins will be demonstrated in 2D and 3D using a 
15 nm X-ray beam. This approach enables visualization of LBT-tagged proteins 
while simultaneously measuring the elemental distribution in cells at a spatial 
resolution necessary for visualizing cell membranes and eukaryotic subcellular 
organelles.


The CBMS Team

-

Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
p 1(631) 344 8375
e nsls.lifescien...@gmail.com
w https://www.bnl.gov/ps/lifesciences/

Address:
Center for Biomolecular Structure
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973





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[ccp4bb] March 24, 2021 - CBMS Lecture Series - Self-Assembling DNA crystal Scafflolds for Arrangement of Biomaterials

[Stojanoff, Vivian]

Exploring Self-Assembling DNA Crystal Scaffolds for the Precise Arrangement of 
Biomaterials

Tara MacCulloch, Arizona State University

 Center for Molecular Design and Biomimetics at the Biodesign Institute



Wednesday March 24; 1:30 pm



LINK:  
https://bnl.zoomgov.com/meeting/register/vJItf-2grT4qHCtWowgMeA6RqJtpusmuG-k

as a confirmation of your registration, you will receive the link to the 
lecture.

Abstract: The foundational goal of structural DNA nanotechnology is to create 
rationally designed crystal lattices to precisely organize macromolecules 
untenable for crystallization to potentially result in the structure of the 
guest species with X-ray crystallography. DNA is ideal for the construction of 
three-dimensional crystals due to its distinctive ability to associate via 
canonical Watson-Crick base pairing which can anneal into a series of “Holliday 
junctions” that are tailed by complementary “sticky ends” which cohere to form 
the 3D arrays. Using these features, the structures of only a handful of these 
DNA scaffolds have been determined. We have recently determined the 2.7 Å 
structure of a prescribed rhombohedral (R3) lattice containing atomic detail 
not previously achieved in any other self-assembled DNA crystal system. The 
role of sticky end sequence was also exhaustively explored to probe its role in 
crystal order, resulting in a related 2.6 Å scaffold. Additionally, we have 
undertaken a comprehensive study of the imperative role that sequence plays at 
each 4-arm junction crossover within the lattice to dictate symmetry and 
resolution, and to allow for the site-specific placement of guest molecules 
with atomic precision. These systems provide significant promise towards the 
construction of improved 3D DNA lattices which could be used as frameworks for 
immobilizing and solving the structure of molecular guests, templating 
catalytic materials, and yield significant insight into the mechanism of DNA 
self-assembly.






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[ccp4bb] CBMS lecture series - March 24, 13:30 EST

[Stojanoff, Vivian]

The Center for Biomolecular Structure cordially invites you to participate in 
their Lecture Series  .





Exploring Self-Assembling DNA Crystal Scaffolds for the Precise Arrangement of 
Biomaterials

Tara MacCulloch, Arizona State University

 Center for Molecular Design and Biomimetics at the Biodesign Institute



Wednesday March 24; 1:30 pm (EST - NY time)



LINK:  
https://bnl.zoomgov.com/meeting/register/vJItf-2grT4qHCtWowgMeA6RqJtpusmuG-k

as a confirmation of your registration, you will receive the link to the 
lecture.

Abstract: The foundational goal of structural DNA nanotechnology is to create 
rationally designed crystal lattices to precisely organize macromolecules 
untenable for crystallization to potentially result in the structure of the 
guest species with X-ray crystallography. DNA is ideal for the construction of 
three-dimensional crystals due to its distinctive ability to associate via 
canonical Watson-Crick base pairing which can anneal into a series of "Holliday 
junctions" that are tailed by complementary "sticky ends" which cohere to form 
the 3D arrays. Using these features, the structures of only a handful of these 
DNA scaffolds have been determined. We have recently determined the 2.7 Å 
structure of a prescribed rhombohedral (R3) lattice containing atomic detail 
not previously achieved in any other self-assembled DNA crystal system. The 
role of sticky end sequence was also exhaustively explored to probe its role in 
crystal order, resulting in a related 2.6 Å scaffold. Additionally, we have 
undertaken a comprehensive study of the imperative role that sequence plays at 
each 4-arm junction crossover within the lattice to dictate symmetry and 
resolution, and to allow for the site-specific placement of guest molecules 
with atomic precision. These systems provide significant promise towards the 
construction of improved 3D DNA lattices which could be used as frameworks for 
immobilizing and solving the structure of molecular guests, templating 
catalytic materials, and yield significant insight into the mechanism of DNA 
self-assembly.


Kind regards,

Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
p 1(631) 344 8375
e nsls.lifescien...@gmail.com
w https://www.bnl.gov/ps/lsbr/

Address:
Life Science Biomedical Technology Resource
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973




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[ccp4bb] The CBMS Virtual Lecture Series - Lecture February 17, 13:30

[Stojanoff, Vivian]

Dear CCP4 fellows

You are invited to the "The Center for Biomolecular Structure (CBMS)   lecture 
series:

Speaker: Dr Hugh O'Neil
Institution: Center for Structural Molecular Biology, Neutron Scattering 
Division, Oak Ridge National Laboratory
Title: Opportunities for characterizing molecular to mesoscale biological 
processes using neutrons

Register in advance for this meeting:
https://bnl.zoomgov.com/meeting/register/vJItcuGqqT8sHs9v64XyTU_Pz2LQPIV9hMQ

After registering, you will receive a confirmation email containing information 
about joining the meeting.








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[ccp4bb] MX and SAXS - Workbenches @ NSLS II - Center for Biomolecular Structure

[Stojanoff, Vivian]

Dear CCP4 Researchers,

The Center for Biomolecular Structure (CBMS) at the National Synchrotron Light 
Source II (https://www.bnl.gov/ps/lifesciences/) is offering two practicals 
workshops on "Solution Scattering" at the LIX beam line and "Macromolecular 
Crystallography" at the A/FMX beam lines from February 8 through February 10. 
The aim of these practical is to provide participants with the current 
practices on data collection and analysis of solution scattering and 
macromolecular crystallography. Scheduled back-to-back participants are 
encouraged to register for both workshops.  Participants are encouraged to send 
their own samples for testing during practicals.

Registration is FREE!  Early registration closes January 25;  Registration 
closes January 29

LIX - Solution Scattering - https://www.bnl.gov/lixworkbench/

A/FMX - Macromolecular crystallography - https://www.bnl.gov/mxworkbench/

Kind regards

Vivian
-
Center for Biomolecular Structure
https://www.bnl.gov/ps/lifesciences/
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973





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[ccp4bb] Solution Scattering and MX workshop November 3 to 5 - Center for BioMolecular Structures

[Stojanoff, Vivian]

You are invited to participate in the Center for BioMolecular Structures  
Solution Scattering - LIX (morning) and Macromolecular Crystallography - MX  
(afternoon) Workbenches,  November 3 through 5. The main goal of these 
workshops is to provide an opportunity to get acquainted with the method and 
software utilized for data collection. Lectures and demonstrations will address 
the capabilities of the beam lines and provide an overview of Structural 
Biology resources available to the community at NSLS II. Tips and Tricks on how 
to collect the best data will be discussed throughout  the workshops. We 
encourage you to send samples and take advantage of the time reserved for the 
workbench to analyze a few samples.

REGISTRATION Deadline: October 23, 2020


https://www.bnl.gov/lixworkbench/


https://www.bnl.gov/mxworkbench/

Please do register for both workshops separately if you plan to participate in 
both. If you do not have a current BNL guest appointment or are planning to 
send samples contact
Vivian Stojanoff (nslsii.lifescie...@gmail.com)

Hope to "see" on November 3rd!

Vivian Stojanoff, PhD
Education, Training, Outreach
User Program - CBMS
p 1(631) 344 8375
e nsls.lifescien...@gmail.com
w https://www.bnl.gov/ps/lifesciences/

Address:
Center for BioMolecular Structures
National Synchrotron Light Source II
Building 745
Brookhaven National Laboratory
Upton NY 11973





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[ccp4bb] NSLS II is accepting Rapid Access Proposals for COVID-19 related research

[Stojanoff, Vivian]

Dear All


Hope that you and your family are doing well,



NSLS-II is offering a streamlined and expedited rapid access proposal process 
for groups that require beam time for structural biology projects directly 
related to COVID-19.


The Center for Biomolecular Structure 
team is supporting remote macromolecular crystallography experiments at the AMX 
and FMX beamlines as well as solution scattering experiments at the LiX 
beamline.



Use the COVID-19 Rapid Access 
form to submit a 
proposal for COVID-19 related research.


Do not hesitate to contact us if we can help with any questions


Kind regards,



Your CBMS Team,

Vivian Stojanoff, PhD
Education, Training, Outreach
User Program
p 1(631) 344 8375
e nsls.lifescien...@gmail.com; 
lifescie...@bnl.gov
w https://www.bnl.gov/ps/lifesciences/
BNL | Center for Biomolecular Structure
The Center is embedded in the National Synchrotron Light Source II (NSLS-II), a 
state-of-the-art synchrotron light source located at the U.S. Department of 
Energy’s (DOE) Brookhaven National Laboratory and adjacent to the Laboratory of 
BioMolecular Structure (LBMS), an advanced cryo-electron microscopy center.
www.bnl.gov





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[ccp4bb] NSLS II COVID-19 related access

[Stojanoff, Vivian]

Dear All


We would like to ensure that NSLS-II (https://www.bnl.gov/ps/), one of the  
brightest X-rays in the world for structural biology research.



To facilitate access to its beam lines  NSLS-II is offering a streamlined and 
expedited rapid access proposal process for groups that require beam time for 
structural biology projects directly related to COVID-19. Please use the 
COVID-19 Rapid Access form 
here.


The Center for Biomolecular Structure 
team is supporting remote macromolecular crystallography experiments at 
Beamlines 17-ID-1 
(AMX) and 17-ID-2 
(FMX) in this research 
area.



For proposal questions, please contact Nancye Wright at 
nsls2u...@bnl.gov. For scientific and/or beamline 
guidance, please contact Sean McSweeney at 
smcswee...@bnl.gov.



We look forward to assisting you with your COVID-19 research project.


Kind Regards,


Vivian Stojanoff






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[ccp4bb] NSLS-II Update and Call for COVID-19 Rapid Access Proposals

[Stojanoff, Vivian]

A message from the NSLS-II Director


Dear NSLS-II Users:

On Monday, March 23, 2020, Brookhaven Lab transitioned to a state of minimum 
operations.  The Lab is expected to operate in this mode until April 14, 2020, 
making further adjustments based on the evolving conditions.  Only Brookhaven 
Lab employees who are essential to operations will be permitted on site during 
this time.

NSLS-II has implemented a plan for minimum-safe operations. In this state, the 
NSLS-II accelerator continues to operate but most of the beamlines have been 
placed in a stand-by mode so that they can be readily re-started when needed 
for critical research, or at an appropriate future date. We have suspended the 
on-site user program at this time; however, our support for the users will 
continue full-time.

First, we are offering a streamlined and expedited rapid access proposal 
process for groups that require beam time for structural biology projects 
directly related to COVID-19. The Center for Biomolecular Structure 
 team is supporting remote macromolecular 
crystallography experiments at Beamlines 17-ID-1 (AMX 
) and 17-ID-2 (FMX 
) in this research 
area.

 In order to submit a macromolecular crystallography proposal for COVID-19 
related research, please use the COVID-19 Rapid Access form here 
.

Second, NSLS-II staff have deployed to full-time telework assignments and 
remain dedicated to supporting users remotely.  We are all still working to 
advance the scientific mission of the facility, so users are encouraged to 
continue working with NSLS-II staff on your projects. We are confident that by 
working together, we will continue to make exciting scientific progress even 
while dispersed and working remotely.

NSLS-II will continue to share information with all of you as our plans evolve. 
 As always, we are happy to answer any questions.  Best wishes and we will look 
forward to seeing you all soon.

Sincerely, and on behalf of the entire NSLS-II staff,

John Hill
Director, NSLS-II







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[ccp4bb] American Crystallographic Association - invitation to submit an abstract

[Stojanoff, Vivian]

We invite you to submit an abstract to the

 Wavelengths and Particles as Tools in Structural Analyses

session scheduled May 26, 2014, Monday morning during the ACA meeting in 
Albuquerque. The focus will be on new applications and methods in X-ray and/or 
neutron crystallography that explore the use of non-conventional wavelengths or 
particle properties, or the wave-particle duality of photons and neutrons for 
structural analyses. Confirmed speakers are: John Helliwell, Dean Myles, B.- C. 
Wang, Wayne Hendrickson.

Two abstracts will be chosen for oral presentation. Abstracts should be 
submitted by Friday, February 7.

The organizers,

B. C. Wang and Vivian Stojanoff

[ccp4bb] Regisytration open The X6A Workbench - February 25-28,2014

[Stojanoff, Vivian]

X6A Workbench: Hands-on Synchrotron Structural Biology
February 25 - 28, 2014
http://workshops.ps.bnl.gov/default.aspx?w=X6AFeb2014


The NIGMS facility at the National Synchrotron Light Source is offering 
comprehensive hands-on training in synchrotron data collection and analysis for 
biophysicists, biochemists and molecular biologists. The goal is to provide 
participants an insight into Structural Biology methods available at a 
synchrotron radiation facility. Four to six participants are invited to follow 
a four day experiment at the X6A beamline. Most of the program will concentrate 
in the development of experimental skills. Introductory lecture will be 
presented by local experts.

Participants are invited to bring their samples for the experiments but samples 
will be provided for training.

Application Deadline is Wednesday, February 19, 2014

For more information, please contact:

Mercy Baez
Photon Sciences User Administration Office
Telephone No.: 631.344.5769tel:631.344.5769
Email Address: b...@bnl.govmailto:b...@bnl.gov

[ccp4bb] X6A Workbench: Hands-on synchrotron structural biology

[Stojanoff, Vivian]

X6A Workbench: Hands-on Synchrotron Structural Biology
June 25 - 28, 2013

The NIGMS facility at the National Synchrotron Light Source is offering 
comprehensive hands-on training in synchrotron data collection and analysis for 
biophysicists, biochemists and molecular biologists. The goal is to provide 
participants an insight into Structural Biology methods available at a 
synchrotron radiation facility. Four to six participants are invited to follow 
a four day experiment at the X6A beamline. Most of the program will concentrate 
in the development of experimental skills. Introductory lecture will be 
presented by local experts.

Participants are invited to bring their samples for the experiments but samples 
will be provided for training.

Application Deadline is Monday, June 17, 2013

For more information, please contact:

Mercy Baez
Photon Sciences User Administration Office
Telephone No.: 631.344.5769
Email Address: b...@bnl.govmailto:b...@bnl.gov

[ccp4bb] registration open for beginners hands-on course on x-ray structural biology

[Stojanoff, Vivian]

The X6A workbench: Advanced Structural Biology Tools??
winter session

(http://protein.nsls.bnl.gov)??

Location: NSLS
Date: March 29 through April 1

We would like to invite you to participate in this four day hands-on course at 
the National Synchrotron Light Source. This course is intended for beginners 
who would like to obtain an overview on macromolecular structure determination. 
This course will discuss the basic concepts of macromolecular crystallography 
beam lines at synchrotron facilities, crystal growth and handling, data 
collection and processing, phasing and the first steps in refinement. Most time 
will be spent at the beam line actually handling crystals and screening for 
cryoprotectants, collecting and processing data at lower energies and at the Se 
edge. Significant amount of time will be spent phasing and obtaining the first 
electron density map.??

Registration; http://protein.nsls.bnl.gov;  you must have an active guest 
appointment at Brookhaven National Laboratory at the time of the course. 

[ccp4bb] The organizers: Frontiers in Automated Crystal Handling and Visualization invite you to participate

[Stojanoff, Vivian]

The Organizers of the workshop:

Frontiers in Automated Crystal Handling and Visualization

May 26-27, 2010

National Synchrotron Light Source, Brookhaven National Laboratorty
Hamilton Conference Room Bldg 555 Chemistry Department


would like to invite you to participate  in this exciting  workshop which will 
discuss the latest happenings  at the 'Frontier in Automated Crystal Handling 
and Visualization'. A panel of distinguished speakers will discuss new methods 
in crystal handling, crystal harvesting, and trends in automatic crystal 
screening,  exploring challenges in micro crystal visualization and handling. A 
detailed agenda can be viewed at:


http://www.nsls.bnl.gov/users/meeting/workshops/workshop.aspx?id=13 .

These trends will influence the concepts for your new MX beam lines at NSLS-II 
(http://www.bnl.gov/nsls2/), the ultra-bright new light source now under 
construction at BNL.  In fact, you may also be interested to help shape the 
beam line proposals by expressing your views in a MX planning group meeting 
that will take place immediately after the workshop in the afternoon of May 27.

For further information please contact one of the organizers,

We are looking forward to seeing you. 

Dieter Schneider (schnei...@bnl.gov), Alexei Soares (soa...@bnl.gov), and 
Vivian Stojanoff (stoja...@bnl.gov)

[ccp4bb] Frontiers in Automated Crystal Handling and Visualization

[Stojanoff, Vivian]

Frontiers in Automated Crystal Handling and Visualization

May 26-27, 2010

National Synchrotron Light Source, Brookhaven National Laboratorty



We invite you to participate in a workshop on 'Frontiers in Automated Crystal 
Handling and Visualization' which we are organizing at Brookhaven National 
Laboratory, May 26 and 27, as part of the 2010 Joint NSLS and CFN Users' 
Meeting. A panel of distinguished speakers will discuss new methods in crystal 
handling, including crystal harvesting, discuss status and trends in automatic 
crystal screening, take stock of evolutions in remote participation, explore 
challenges in micro crystal visualization and handling, and review current 
experiences with automation at micro diffraction beam lines. A detailed agenda 
can be viewed at: 

http://www.nsls.bnl.gov/users/meeting/workshops/workshop.aspx?id=13 .

These trends will influence the concepts for your new MX beam lines at NSLS-II 
(http://www.bnl.gov/nsls2/), the ultra-bright new light source now under 
construction at BNL.  In fact, you may also be interested to help shape the 
beam line proposals by expressing your views in a MX planning group meeting 
that will take place immediately after the workshop in the afternoon of May 27.

To register http://www.nsls.bnl.gov/users/meeting/page.aspx?id=home 

We are looking forward to seeing soon at BNL,

Dieter Schneider (schnei...@bnl.gov), Alexei Soares (soa...@bnl.gov), and 
Vivian Stojanoff (stoja...@bnl.gov)

the organizers.

[ccp4bb] The X6A workbench winter session

[Stojanoff, Vivian]

The X6A workbench: Advanced Structural Biology Tools

(http://protein.nsls.bnl.gov)

We would like to invite you to participate in this four day hands-on course at 
the NIGMS Research Facility at the National Synchrotron Light Source. This 
course is intended for beginners who would like to obtain an overview on 
macromolecular structure determination. This course will discuss the basic 
concepts of macromolecular crystallography beam lines at synchrotron 
facilities, crystal growth and handling, data collection and processing, 
phasing and the first steps in refinement. Most time will be spend at the beam 
line actually handling crystals and screening for cryoprotectants, collecting 
and processing data. Significant amount of time is spent phasing and obtaining 
the first electron density map.

Registration; http://protein.nsls.bnl.gov;  you must have an active guest 
appointment at Brookhaven National Laboratory at the time of the course.  

[ccp4bb] Postdoctoral position at Brookhaven National Laboratory

[Stojanoff, Vivian]

POST DOCTORAL RESEARCH ASSOCIATE

The National Institute of General Medical Sciences East Coast Structural 
Biology Research Facility, X6A beam line at the NSLS, Brookhaven National 
Laboratory has an immediate opening for Postdoctoral Research Associate 
position. Funded by the National Institute of General Medical Sciences the X6A 
beam line is dedicated to macromolecular crystallography. The successful 
candidate will have a PhD degree in chemistry, physics, biochemistry or related 
subject,  experience in structure determination and background in X-ray 
diffraction techniques. Knowledge in protein cloning, expression and 
purification would be beneficial.  The selected candidate will work as part of 
a multidisciplinary research team on projects focused on the understanding of 
structural functional determinants in the design of chemical epigenomic probes. 
He or she will join members of the NIGMS ECSBRF at beam line X6A in the 
development and implementation of X-ray diffraction methods, as well as, assist 
in the s!
 upport of the X6A User Program. The candidate should have good communication, 
organizational and time management skills. To apply please email: 1. CV 2. 
statement of interests, and 3. names and addresses of three references to  
Vivian Stojanoff: stojan...@bnl.gov. Brookhaven National Laboratory (BNL) is a 
Federally Funded Research and Development Center (FFRDC) for research in the 
physical, biomedical and applied sciences.  It is operated by Brookhaven 
Science Associates, a non-profit management corporation, under the terms of a 
prime contract with the U.S. Department of Energy. BNL policy states that Post 
Doctoral appointments may be made to those who have received their doctoral 
degrees within the past five years. 

Contact information:
Brookhaven National Laboratory
National Synchrotron Light Source
Dr. Vivian Stojanoff
stojan...@bnl.gov
http://protein.nsls.bnl.gov

[ccp4bb] The X6A workbench: Advanced Structural Biology Tools, is back!

[Stojanoff, Vivian]

Yes!  The X6A workbench: Advanced Structural Biology Tools,   is back. 

The next session is scheduled for: June 9 through 12, 2009

http://protein.nsls.bnl.gov

We would like to invite you to participate in this four day hands-on course at 
the NIGMS Research Facility at the National Synchrotron Light Source. This 
course is intended for beginners who would like to obtain an overview on 
macromolecular structure determination. The course includes lectures on 
synchrotron and beam line hardware, crystal growth and handling, data 
collection and processing, phasing and the first steps in model building and 
refinement. The main sessions of the workshop will consist of hands-on 
experience at the beam line actually handling crystals and screening for 
cryoprotectants, collecting and processing data. Significant amount of time is 
spent phasing and obtaining the first electron density map.

Registration; http://protein.nsls.bnl.gov; you must have an active guest 
appointment at Brookhaven National Laboratory at the time of the course.  An 
updated schedule will be posted on the website of the course by the end of May, 
2009. 

For further information contact:
Vivian Stojanoff
Phone: +1 631 344 8375 
or 
Jean Jakoncic
Phone: +1 631 344 3930

[ccp4bb] Beam time available @X6A NSLS

[Stojanoff, Vivian]

Beam time available @ X6A

http://protein.nsls.bnl.gov


The NIGMS beam line X6A at the National Synchrotron Light Source has recently 
replaced its end-station. The beam line now operates a ADSC Q270  CCD detector 
and  a Crystallogic diffractometer equipped with an air-bearing single rotation 
axis. For screening large numbers of sample an  ALS like  automounted sample 
changer capable of screen 16 samples in 40 minutes is available upon request.

Beam time can be scheduled as fast as making reservations for a trip. Just 
locate the available beam time on the schedule and use the drop down menu to 
select the date that fits best into your schedule. Of course you need to have a 
project first, but this is easy too.. just submit a small abstract 
(http://protein.nsls.bnl.gov) and your project will be reviewed within a few 
days. 

If you like to know more 

send an email:

x6an...@bnl.gov

or call:

+1 (631) 344 8375




Vivian Stojanoff
National Synchrotron light Source
Brookhaven National Laboratory
Bldg 725D
Upton, NY 11973 USA
Email: stoja...@bnl.gov;vivian.stojan...@gmail.com
phone: +1 631 344 8375
fax:  +1 631 344 3238

[ccp4bb] Beam time available @ the NIGMS beam line at the NSLS

[Stojanoff, Vivian]

Beam time available @ X6A 

http://protein.nsls.bnl.gov


The NIGMS beam line X6A at the National Synchrotron Light Source provides FAST 
access to beam time through out the year. To apply submit a short proposal to 
http://protein.nsls.bnl.gov   at any time. Proposals are continuously reviewed 
and beam time can be scheduled within a week.

For comments or further questions please contact the scientific staff at:
x6an...@bnl.gov
or call:
+1 (631) 344 8375


-

Vivian Stojanoff
National Synchrotron light Source
Brookhaven National Laboratory
Bldg 725D
Upton, NY 11973 USA
Email: stoja...@bnl.gov; stoja...@yahoo.com
phone: +1 631 344 8375
fax:  +1 631 344 3238

[ccp4bb] Crystallization focus on membrane proteins 2008 - Registration deadline JUNE 2nd

[Stojanoff, Vivian]

Dear colleagues,


Crystallization: focus on membrane protein 2008

June 18 - 22, 2008, Brookhaven National Laboratory, Upton, NY

http://www.nsls.bnl.gov/newsroom/events/workshops/2008/crys/default.asp

DEADLINE for REGISTRATION: June 2, 2008.

Topics include membrane protein purification, solubilization and detergent 
screening and compatibility, 3D crystallization, QLTS, cryoprotection and 
diffraction quality determination. Participants will be able to experiment 
different crystal growth methods, vapor, lipid cubic phase, gel, microfluidics, 
and dialysis during the course.

For further information, please see to the course website

Best regards

Vivian Stojanoff
Brookhaven National Laboratory
National Synchrotron Light Source
Upton NY 11973 USA

Phone: +1 631 344 8375 (office)
email:  [EMAIL PROTECTED]
http://protein.nsls.bnl.gov

[ccp4bb] Crystallization focus on membrane proteins 2008 - Preliminary agenda

[Stojanoff, Vivian]

Dear colleagues,

The preliminary agenda for the course

Crystallization: focus on membrane protein 2008 

June 18 - 22, 2008, Brookhaven National Laboratory, Upton, NY

is now available and can be viewed at: 

http://www.nsls.bnl.gov/newsroom/events/workshops/2008/crys/agenda.asp


Topics include membrane protein purification, solubilization and detergent 
screening and compatibility, 3D crystallization, QLTS, cryoprotection and 
diffraction quality determination. Participants will be able to experiment 
different crystal growth methods, vapor, lipid cubic phase, gel, microfluidics, 
and dialysis during the course. 

Participants are encouraged to bring their own samples and experiment during 
the course.

For further information, please see to the course website

http://www.nsls.bnl.gov/newsroom/events/workshops/2008/crys

Please register online.

Best regards

Vivian Stojanoff
Brookhaven National Laboratory
National Synchrotron Light Source
Upton NY 11973 USA

Phone: +1 631 344 8375 (office)
email:  [EMAIL PROTECTED]
   http://protein.nsls.bnl.gov

[ccp4bb] Crystallization: Focus on Membrane Proteins 2008

[Stojanoff, Vivian]

LAST DAYS to APPLY to the IUCr sponsored TRAVEL GRANT

Extended Deadline
http://www.nsls.bnl.gov/newsroom/events/workshops/2008/crys/


To apply for the IUCr sponsored Travel Grant to participate in the 
Crystallization: Focus on Membrane Proteins 2008
course you must register for the course and send:

- short statement of interest
- a short CV
- a recomendation from your supervisor or department head

to 

Vivian Stojanoff
Brookhaven National Laboratory 
National Synchrotron Light Source
Bldg 725D
Upton NY 11973

or in pdf format by email:

[EMAIL PROTECTED]

[ccp4bb] Crystallization 2008 - IUCr Travel Grant last days to apply

[Stojanoff, Vivian]

Crystallization: Focus on Membrane Proteins

June 18-22, 2008

http://www.nsls.bnl.gov/newsroom/events/workshops/2008/crys/

A grant from The International Union of Crystallography will support the 
attendance of a limited number of attendees. Preference will be given to Young 
Scientists [graduate students, post-graduate students or post-doctoral fellows 
with a maximum age of 30 (exceptionally 35)] from developing countries. 
To be elligible you must have registered for the Course and applied for a BNL 
guest appointment.

Please send your application including:

 a short letter stating your interest and your goals in attending this course
 a short resume
 a letter from your thesis advisor or department supervisor

to Vivian Stojanoff, Brookhaven National Laboratory, National Synchrotron Light 
Source, Bldg 725D, Upton NY 11973, USA, by May 10th. Travel Grant Recipients 
will be notified by May 15th. 

In accordance with the standards of the International Union of Crystallography, 
we observe the basic policy of non-discrimination, affirming the right and 
freedom of scientists to associate in international scientific activity without 
regard to such factors as citizenship, religion, creed, political stance, 
ethnic origin, race, color, language, age, or gender, in accordance with the 
Statutes of the International Council for Science. At this course no barriers 
will exist beyond the application procedure that would prevent the 
participation of bona fide scientists.

[ccp4bb] Crystallization: focus on memebrane proteins 2008

[Stojanoff, Vivian]

Crystallization: Focus on Membrane Proteins
June 18-22, 2008

http://www.nsls.bnl.gov/newsroom/events/workshops/2008/crys/

Purpose  Scope of Workshop:
The purpose of this course is to provide participants with hands-on experience 
of a variety of crystal growth methods. The course will address both 
conventional and non-conventional methods in membrane proteins. Introductory 
lectures will precede the practical sessions. Time for discussions and informal 
meeting with speakers and  tutors is scheduled. Participants will be divided 
into groups of four to five members according to their main interests and 
follow practical sessions during the course.A special session on cryogenic 
protection and crystal quality assessment of crystals will be conducted at the 
X6A beam line on the last day.

Intended Audience
Graduate students, post-doctoral fellows and research scientists interested in 
learning about different approaches to crystallization.

Selection Criteria
There is no selection criteria. The inclusion of a small resume and a statement 
of interest with the registration form are strongly recommended, as groups will 
be organized according to their common level.

Travel Grants
A grant from The International Union of Crystallography will support the 
attendance of a limited number of attendee's. Preference will be given to Young 
Scientists [graduate students, post-graduate students or post-doctoral fellows 
with a maximum age of 30 (exceptionally 35)] from developing countries. 
For additional inofrmation refer to the course webpages: 
http://www.nsls.bnl.gov/newsroom/events/workshops/2008/crys/ or contact the 
organizers.


In addition to submitting an Application Form for this workshop, all attendees 
must obtain a BNL guest appointment. Please register in BNL's Guest Information 
System  (https://fsd84.bis.bnl.gov/guest/guest.asp). Approval, which can take 
30 days or more, must be granted prior to attending this workshop.


Travel Grants

A grant from The International Union of Crystallography will support the 
attendance of a limited number of attendee's. Preference will be given to Young 
Scientists [graduate students, post-graduate students or post-doctoral fellows 
with a maximum age of 30 (exceptionally 35)] from developing countries. 

[ccp4bb] X6A @ NSLS: Beam time available

[Stojanoff, Vivian]

Beam time available @ X6A

http://protein.nsls.bnl.gov


The NIGMS beam line X6A at the National Synchrotron Light Source provides FAST 
access to beam time through out the year. To apply submit a short proposal to 
http://protein.nsls.bnl.gov   at any time. Proposals are continuously reviewed 
and beam time can be scheduled within a week.

For comments or further questions please contact the scientific staff at:

[EMAIL PROTECTED]
or call:
+1 (631) 344 8375


Vivian Stojanoff
National Synchrotron light Source
Brookhaven National Laboratory
Bldg 725D
Upton, NY 11973 USA
Email: [EMAIL PROTECTED]; [EMAIL PROTECTED]
phone: +1 631 344 8375
fax:  +1 631 344 3238

[ccp4bb] Beam Time Available @X6A

[Stojanoff, Vivian]

The NIGMS East Coast Structural Biology Facility has beam time for fast access 
starting October 13. 

Available time can be checked through the link bellow

http://protein.nsls.bnl.gov 

Do you have  a project or if you want to submit a new project you will be able 
to schedule your own beam time using the X6A web based calendar. 

If you have any questions contact the beam line staff at: 


Brookhaven National Laboratory 
National Synchrotron Light Source 
Bldg725D 
Upton NY 11973 USA 

Phone: +1 631 344 8375 
  +1 631 344 5836 

email:  [EMAIL PROTECTED]; [EMAIL PROTECTED] 
  http://protein.nsls.bnl.gov 

[ccp4bb] The X6A workbench - Fall session

[Stojanoff, Vivian]

The X6A workbench - Advanced Strucutral Biology Tools

at the National Synchrotron Light Source

scheduled for September 25 through 28


Is a hands-on course for those interested in getting acquainted with 
Synchrotron Radiation methods in structural biology.
The course provides a comprehensive view of data collection and data analysis 
aspects of a synnchrotron experiment. 
The number of participants is limited to six as the program concentrates on the 
development of experimental skills. 

Further information can be found through the link

http://protein.nsls.bnl.gov/mediawiki/index.php/X6A_Workbench

[ccp4bb] NSLSII User Workshop - July 17-18,2007 - Macromolecular Crystallography

[Stojanoff, Vivian]

As part of the NSLS-II USER WORKSHOP 

https://www.bnl.gov/nsls2meeting/

hosted by the Brookhaven National Laboratory (Upton, NY) several sessions on 
Life Sciences are being planned, including a breakout session on: 

MACROMOLECULAR CRYSTALLOGRAPHY  

We would like to invite members of the community to participate in this session 
planned for July 18th.

The aim of the Macromolecular Crystallography breakout session is to discuss 
how the unique features presented by the planned NSLSII storage ring can best 
contribute to further the understanding of  molecular structures and 
bio-molecular functions. The two hour workshop is divided into two parts: an 
introductory part featuring scientific and instrumentation development talks; 
and a second part including an open discussion between members of the audience 
on the specific future scientific needs of the field and instrumentation 
resources.  For further information follow the link: 
https://www.bnl.gov/nsls2meeting/ or contact one of the session organizers, Bob 
Sweet ([EMAIL PROTECTED]) or Vivian Stojanoff ([EMAIL PROTECTED])

Vivian Stojanoff
For the session organizing committee


 

[ccp4bb] Crystallization Course: focus on membrane proteins 2007- Final Agenda

[Stojanoff, Vivian]

Crystallization Course:focus on membrane proteins 2007

http://www.nsls.bnl.gov/newsroom/events/workshops/2007/crys/

The final agenda for the Crystallization Course:focus on membrane proteins 2007
is now available of the course web site.

The purpose of this course is to provide participants with hands-on 
experience of a variety of crystal growth methods for obtaining high 
quality crystals. The course will address both conventional and 
non-conventional methods in membrane protein crystal growth. 

Limited support will be offered by a travel grant provided by the IUCr 
to young scientists. Application deadline May 31st.

 

[ccp4bb] Crystallization Course: focus on membrane proteins 2007

[Stojanoff, Vivian]

Crystallization: focus on membrane proteins.

http://www.nsls.bnl.gov/newsroom/events/workshops/2007/crys/

The Crystallization Course at Brookhaven National Laboratory this year will 
focus on membrane proteins.
Sponsored by the IUCr the purpose of the course is to provide participants with 
hands-on
experience of a variety of crystal growth methods. The course will
address both conventional and non-conventional methods in membrane
proteins. Optimization methods will include application of oils, novel
nucleating agents, detergents, crystallization in lipid cubic phase,
crystallization with gels , microfluidics, and more...

Introductory lectures will precede the practical sessions. Time for
discussions and informal meeting speakers and  tutors is scheduled.
Speakers and tutors:

Marcia Amstrong (Qiagen)
Neer Asherie (Yeshiva University)
Bert van den Berg (Massachussets University)
Troy Burke (GE Healthcare)Mark Elliot (Emerald BioSystems), TBC
Ingo Grotjohann (Arizona State University), TBC
Trevor Harvard (Precision Detectors)
Rustem Ismagilov (Chicago University), TBC
Liang Li ( Chicago University), TBC
Patrick J. Loll (Drexel University)
Marie-Claude Marchand (Qiagen), TBC
Abel Moreno (Universidad Nacional Autonoma de Mexico)
Gweneth Nneji (Birbeck University of London)
Peter Nollert (Emerald BioSystems)
Michael C. Wiener (University of Virginia), TBC

Limited Travel assitance is provided by the International Union of 
Crystallography. Please check the Course site for further details or contact:

Vivian Stojanoff
Brookhaven National Laboratory
National Synchrotron Light Source
Bldg725D
Upton NY 11973 USA

Phone: +1 631 344 8375 (office)
  +1 631 344 5836 (X6A beam line)
Fax:+1 631 344 3238
email:  [EMAIL PROTECTED], 
  http://protein.nsls.bnl.gov

Rapid Access to beam time @X6A

[Stojanoff, Vivian]

Beam time available @ X6A NSLS

http://protein.nsls.bnl.gov


The NIGMS beam line X6A provides rapid access to bema time throughout the 
yearr.  If you already submitted a project just find a time that fits your 
schedule, if you are working on new projects why not get ready for scheduling 
and by submitting your project now. The submission of a project is as simple as 
1 2 3. You need just a few sentences to describe the importance and motivation 
and a couple of more sentences describing the current status. If you have 
comments or further questions please contact us at:

[EMAIL PROTECTED]
or call:
+1 (631) 344 8375


NEXT BEAM TIME AVAILABLE  FEBRUARY 2nd 


Vivian Stojanoff
National Synchrotron light Source
Brookhaven National Laboratory
Bldg 725D
Upton, NY 11973 USA
Email: [EMAIL PROTECTED]; [EMAIL PROTECTED]
phone: +1 631 344 8375
fax:  +1 631 344 3238