[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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Re: [ccp4bb] disordered cysteine

[MARCHOT Pascale]

Hello,
A bibliography search with keywords "radiation damage disulfide" retrieves a 
long list of examples and reviews
Best wishes - PM


De : CCP4 bulletin board  de la part de Maria Håkansson 

Envoyé : lundi 22 avril 2024 13:25
À : CCP4BB@JISCMAIL.AC.UK
Objet : Re: [ccp4bb] disordered cysteine


Ce mail provient de l'extérieur, restons vigilants

Dear Oliviero,

For sure cysteines can be disordered.
Sometimes you can find one conformation reduced and another conformation 
oxidised if the cysteine
is solvent exposed. Also in well-resolved structures you can see a cysteine 
taking part in a disulphide bond,
but only partially, one conformation being unbound. This can have to do with 
how you treated your protein
with reducing agents but probably also depend on how easily reduced the 
disulphide bond is.
Also cysteines can be modified by beta-mercaptoethanol if this chemical is 
added in large amounts and the cysteines are solvent exposed.
More seldom I have seen double conformation alone of cysteines but I guess this 
may occur as well.

It can be difficult to correctly model oxidised and reduced or native cysteines 
in the same residue since the
residue names differ (and you can only have one name). Depending on occupancy I 
usually use CYS only if
lower occupancy of the oxidised form or if higher occupancy of the oxidised 
form CSO for both (could be other species too),
possibly with zero occupancy on the oxygen missing. Maybe there is better 
suggestions?

Sorry not to be able to share any references.

Good luck!

Best regards,
Maria



On 22 Apr 2024, at 10:55, Italo Carugo Oliviero  
wrote:

Dears,
is it possible for a cysteine to be conformationally disordered? It seems 
strange to me. If it were, it would almost certainly be exposed to the solvent 
and thus easily oxidized irreversibly. Do you perhaps have any information on 
conformationally disordered cysteines?
I thank you,
Oliviero



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Maria Håkansson, PhD,
Principal Scientist

SARomics Biostructures AB
Medicon Village
SE-223 81 Lund, Sweden

Mobile: +46 (0)76 8585706
Web: www.saromics.com








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Re: [ccp4bb] disordered cysteine

[Maria Håkansson]

Dear Oliviero,

Resending the message since I am not sure you got it.

For sure cysteines can be disordered.
Sometimes you can find one conformation reduced and another conformation 
oxidised if the cysteine
is solvent exposed. Also in well-resolved structures you can see a cysteine 
taking part in a disulphide bond,
but only partially, one conformation being unbound. This can have to do with 
how you treated your protein
with reducing agents but probably also depend on how easily reduced the 
disulphide bond is.
Also cysteines can be modified by beta-mercaptoethanol if this chemical is 
added in large amounts and the cysteines are solvent exposed.
More seldom I have seen double conformation alone of cysteines but I guess this 
may occur as well.

It can be difficult to correctly model oxidised and reduced or native cysteines 
in the same residue since the
residue names differ (and you can only have one name). Depending on occupancy I 
usually use CYS only if
lower occupancy of the oxidised form or if higher occupancy of the oxidised 
form CSO for both (could be other species too),
possibly with zero occupancy on the oxygen missing. Maybe there is better 
suggestions?

Sorry not to be able to share any references.

Good luck!

Best regards,
Maria


> On 22 Apr 2024, at 10:55, Italo Carugo Oliviero 
>  wrote:
> 
> Dears,
> is it possible for a cysteine to be conformationally disordered? It seems 
> strange to me. If it were, it would almost certainly be exposed to the 
> solvent and thus easily oxidized irreversibly. Do you perhaps have any 
> information on conformationally disordered cysteines?
> I thank you,
> Oliviero
> 
> To unsubscribe from the CCP4BB list, click the following link:
> https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB=1
> 

Maria Håkansson, PhD,
Principal Scientist

SARomics Biostructures AB
Medicon Village
SE-223 81 Lund, Sweden

Mobile: +46 (0)76 8585706
Web: www.saromics.com








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Re: [ccp4bb] disordered cysteine

[Maria Håkansson]

Dear Oliviero,

For sure cysteines can be disordered.
Sometimes you can find one conformation reduced and another conformation 
oxidised if the cysteine
is solvent exposed. Also in well-resolved structures you can see a cysteine 
taking part in a disulphide bond,
but only partially, one conformation being unbound. This can have to do with 
how you treated your protein
with reducing agents but probably also depend on how easily reduced the 
disulphide bond is.
Also cysteines can be modified by beta-mercaptoethanol if this chemical is 
added in large amounts and the cysteines are solvent exposed.
More seldom I have seen double conformation alone of cysteines but I guess this 
may occur as well.

It can be difficult to correctly model oxidised and reduced or native cysteines 
in the same residue since the
residue names differ (and you can only have one name). Depending on occupancy I 
usually use CYS only if
lower occupancy of the oxidised form or if higher occupancy of the oxidised 
form CSO for both (could be other species too),
possibly with zero occupancy on the oxygen missing. Maybe there is better 
suggestions?

Sorry not to be able to share any references.

Good luck!

Best regards,
Maria



> On 22 Apr 2024, at 10:55, Italo Carugo Oliviero 
>  wrote:
> 
> Dears,
> is it possible for a cysteine to be conformationally disordered? It seems 
> strange to me. If it were, it would almost certainly be exposed to the 
> solvent and thus easily oxidized irreversibly. Do you perhaps have any 
> information on conformationally disordered cysteines?
> I thank you,
> Oliviero
> 
> To unsubscribe from the CCP4BB list, click the following link:
> https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB=1
> 

Maria Håkansson, PhD,
Principal Scientist

SARomics Biostructures AB
Medicon Village
SE-223 81 Lund, Sweden

Mobile: +46 (0)76 8585706
Web: www.saromics.com








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[ccp4bb] Postdoctoral Researcher for SSX-driven fragment screening at MicroMAX (MAX IV)

[Tobias Krojer]

Dear all,

We are looking for a postdoctoral researcher for a two-year position dedicated 
to advancing serial crystallography fragment screening at our brand-new 
MicroMAX beamline. This role offers a unique collaboration with the FragMAX 
team to seamlessly integrate cutting-edge methods into routine use at our 
facility. The successful candidate will be supported by the MX group's 
extensive and varied expertise. Additionally, the position entails frequent 
exchanges with scientists from DESY, the University of Hamburg, and the 
University of Gothenburg. This is an exceptional opportunity for a creative and 
driven scientist eager to rethink the application of X-ray crystallography in 
structure-based drug discovery.
You can find more information about the position and instructions about how to 
apply here:
https://lu.varbi.com/en/what:job/jobID:717582
The application deadline is Sunday, 05. May 2024.
Please feel free to contact Thomas Ursby 
(thomas.ur...@maxiv.lu.se) or me 
(tobias.kro...@maxiv.lu.se) if you have any 
questions about the position.
Best,
Tobias


--

[signature_915632486]

Dr. Tobias Krojer
FragMAX Team Leader

MAX IV Laboratory
Lund University
P.O.Box 118, SE-221 00 Lund, Sweden
Visiting address: Fotongatan 2, 22484 Lund
tobias.kro...@maxiv.lu.se
Mobile: +46 79 066 0189
Phone: +46 46 2226779
www.maxiv.se





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[ccp4bb] disordered cysteine

[Italo Carugo Oliviero]

Dears,
is it possible for a cysteine to be conformationally disordered? It seems
strange to me. If it were, it would almost certainly be exposed to the
solvent and thus easily oxidized irreversibly. Do you perhaps have any
information on conformationally disordered cysteines?
I thank you,
Oliviero



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[ccp4bb] PDRA available at Kings College London

[Elspeth Garman]

Dear BBers
I am posting this PDRA advert on behalf of Prof James McDonnell at Kings 
College London.
The advertisement is below, or can also be found at LinkedIn 
https://www.linkedin.com/jobs/view/3894686078
Best wishes
Elspeth
Structure-based drug discovery in immunology, King's College London, The 
Randall Centre for Cell & Molecular Biophysics
The role
We seek a talented, highly motivated and independent Postdoctoral Research 
Associate (fixed-term) to study antibody structure and function at King's 
College London. Work will be carried out in the laboratory of Professor James 
McDonnell in the Randall Centre for Cell and Molecular Biophysics within the 
Faculty of Life Sciences and Medicine at King's College London. This full-time 
fixed term post is part of a joint programme with industrial collaborator 
Apollo Therapeutics. The successful applicant will join an interdisciplinary 
team studying the structure, molecular interactions and functions of 
antibodies. The Researcher will be part of a team using structure-based methods 
to develop novel inhibitory agents of antibodies. Successful applicants will 
have experience in X-ray crystallographic studies of proteins and protein 
complexes. Structural methods will be a core component of this research 
project, and these approaches will be complemented by biochemical and 
biophysical experiments.
This post will be offered on an a fixed-term contract for 1 year in the first 
instance
This is a full-time post - 100% full time equivalent.
Further details about the post can be found at: 
https://www.kcl.ac.uk/jobs/087505-research-associate
Salary: £43,205 to £44,347 per annum, including London Weighting Allowance.
Closing Date: 29 April, 2024 Informal enquiries can be made to Professor James 
McDonnell (james.mcdonn...@kcl.ac.uk)

Elspeth F. Garman,
Professor of Molecular Biophysics (Emerita),
Supernumerary Fellow (Emerita), Brasenose College, University of Oxford
Postal address:
  Department of Biochemistry
  Dorothy Crowfoot Hodgkin Building
  Oxford, OX1  3QU, U.K
E-mail: elspeth.gar...@bioch.ox.ac.uk
https://www.bioch.ox.ac.uk/garmangroup
   -




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