[ccp4bb] Five Postdoctoral Positions at Oak Ridge National Laboratory

2012-09-04 Thread Leighton Coates
Five Postdoctoral Research Associates in Molecular Biology and
Macromolecular Crystallography

Reference Code ORNL12-87-BSMD

Eligibility Requirements

Degree: Currently pursuing a Doctoral Degree  or have received this
Degree within 60 months.

Description
The Neutron Sciences Directorate (NScD) at Oak Ridge National
Laboratory operates the High Flux Isotope Reactor (HFIR), the United
States highest flux reactor based neutron source, and the Spallation
Neutron Source (SNS), the world's most intense pulsed accelerator
based neutron source. Together these facilities operate 24 instruments
for neutron scattering research, each year carrying out 1000 experiments in the
physical, chemical, materials, biological and medical sciences for 2000 visiting
scientists. HFIR also provides unique facilities for isotope production and
neutron irradiation. To learn more about Neutron Sciences at ORNL go
to: http://neutrons.ornl.gov.

The Biology and Soft Matter Division at Oak Ridge National Laboratory
(ORNL) invites applications for up to 5 positions for
biochemist/molecular biologists and macromolecular crystallographers.
The successful
candidates will carry out research investigating the structure and
function of several biological systems, including human cAMP dependent protein
kinases, plant cellulose synthase complexes, and bioenergy related
enzymes involved in isomerization and epimerization reactions.  These
projects involve multi-task, multi-disciplinary efforts involving
molecular biology, protein crystallography, small–angle scattering, rational
design using computer modeling techniques, and enzymology. The
positions represent an excellent opportunity for researchers to develop their
careers and interact with leading scientists from around the world.


Qualifications
A Ph.D. degree in structural biology or a related field is required.
The candidates should have a proven track record in molecular biology
techniques including, plasmid-based heterologous protein expression,
protein purification, protein crystallographic data collection, and
structure determination and refinement. Expertise in isotopic
labeling, eukaryotic expression systems, and biofermentation would be
a distinct advantage. The candidates should be self-motivated, have good
interpersonal, communication and presentational skills and
demonstrated ability to interact effectively with staff at all levels
and to work within a multi-disciplinary team.

Required disciplines:  Structural Biology, Biochemistry, Molecular Biology.

Questions regarding these positions can be directed to Dr. Hugh
O’Neill (oneil...@ornl.gov); Dr. William Heller (helle...@ornl.gov);
Dr Leighton Coates (coat...@ornl.gov) or Dr. Paul Langan (langa...@ornl.gov).

Applicants cannot have received the most recent degree more than five
years prior to the date of application and must complete
all degree requirements before starting their appointment.


Number of Openings 5

Program Postgraduate

Division Biology and Soft Matter

Academic Levels
Postdoctoral


[ccp4bb] Associate Division Director for Structural Biology at NSLS-II

2012-09-04 Thread Miller, Lisa M
Associate Division Director for Structural Biology
National Synchrotron Light Source II
Brookhaven National Laboratory

The Photon Sciences Directorate at Brookhaven National Laboratory is seeking an 
experienced and internationally recognized scientist to fill a new leadership 
position as Associate Division Director (ADD) for Structural Biology in the 
Photon Division. Reporting to the Division Director, the ADD for Structural 
Biology will work closely with the Chief Life Scientist to lead the Photon 
Sciences effort to plan, develop, and conduct a highly productive and 
high-impact structural biology program at NSLS-II structural biology beamlines 
covering a suite of techniques from macromolecular crystallography to X-ray 
scattering. NSLS-II is a new third generation synchrotron facility being 
constructed on Long Island, New York with extremely high brightness and 
exceptional beam stability that are expected to benefit the structural biology 
program.

Specific roles and responsibilities include:
*   Leading the effort in planning and implementing structural biology 
beamlines and supporting facilities and associated scientific programs, 
including interacting with various stakeholders such as the scientific user 
community and funding agencies
*   Coordinating and overseeing  structural  beamline development, upgrade, 
and operation activities with scientists and user communities, including 
oversight of partner user programs and staff beam time usages
*   Managing all aspects of staffing and budgetary resources of the 
Structural Biology Program including workforce planning, developing, 
recommending, and implementing approved staffing and budgetary plans as required
*   Conducting a research program in structural biology, methodology, or 
synchrotron instrumentation
*   Ensuring a safe, positive, and productive working environment

Qualifications Required:
*   Ph.D. in biochemistry, biophysics, or a related field
*   Minimum of 10 years of working experience associated with managing or 
developing synchrotron-based structural biology programs or facilities
*   Experience in synchrotron-based research in structural biology
*   Excellent written and oral communication skills
*   The ability to interact effectively in a team environment with a 
diverse group of scientists, engineers, technical staff, users, and other 
stakeholders

Qualifications Preferred:
*   Active research program in structural biology or in methodology or 
synchrotron instrumentation
*   Experience with grant writing and demonstrated success in securing 
research funding
*   Prior experience in managing construction and/or operation of a 
synchrotron beamline or instrumentation, including project planning, execution, 
reporting, and budget and resource management

At Brookhaven National Laboratory we believe that a comprehensive employee 
benefits program is an important and meaningful part of the compensation 
employees receive. Our benefits program includes but is not limited to: Medical 
Plans, Vacation, Holidays, Dental Plans, Life Insurance, 401(k) Plan, 
Retirement Plan, On-site Child Development Center, swimming pool, weight room, 
tennis courts and many other employee perks and benefits. BNL is an Affirmative 
Action/Equal Opportunity Employer committed to the development of a diverse 
workforce.

Please visit http://www.bnl.gov/HR/careers/ and apply to Job ID# 16185
For questions, please contact Dr. Qun Shen at 
qs...@bnl.govmailto:qs...@bnl.gov or Mr. Peter Esposito at 
petere...@bnl.govmailto:petere...@bnl.gov






[ccp4bb] Determining Rpim value

2012-09-04 Thread Michelle Deaton
I am trying to obtain an Rpim (precision indicating merging Rfactor) value
for a dataset that I have already processed with HKL2000/Scalepack and
refined.  Is there a straightforward way to obtain this value from my
data?  From what I understand, most of my options involve going back and
obtaining unmerged intensities.  I am hoping there may be a way for me to
avoid having to backtrack that far, as this data is now very far along in
the refinement process.

Thank you,
Michelle Deaton

University of Denver
Department of Chemistry and Biochemistry


Re: [ccp4bb] Determining Rpim value

2012-09-04 Thread Phil Jeffrey
If the alternative to reprocessing your data with XDS, iMosflm, Xia2, 
autoProc etc is unpalatable, might I suggest the nearly-as-unpalatable 
method as follows:


If you can still run Scalepack on all your .x files, put the line
NO MERGE ORIGINAL INDEX
in the scalepack script file.  Get the .sca or .hkl file out of that.
Use the following - strictly no warranties - script:

#  Assumes scalepack.hkl is created with NO MERGE ORIGINAL INDEX
#
#
pointless SCAIN scalepack.hkl HKLOUT scalepack.mtz  EOF
NAME PROJECT mydata CRYSTAL mydata1
CELL 75.2   75.2   135.890.00090.00090.000
EOF
#
#
scala hklin scalepack.mtz hklout scala.mtz \
  scales   scala.scales \
  rogues   scala.rogues \
  normplot scala.norm \
  anomplot scala.anom EOF
bins 20
resolution 2.9
run 1 all
resolution run 1 high 2.9
name run 1 project AUTOMATIC crystal DEFAULT dataset scalepack
scales constant
exclude sdmin 2.0
sdcorrection fixsdb noadjust norefine both 1.0 0.0
anomalous off
EOF

Corrections, comments or outright repudiation of this script quite 
welcome - this was my first attempt.


Phil Jeffrey
Princeton


On 9/4/12 6:14 PM, Michelle Deaton wrote:

I am trying to obtain an Rpim (precision indicating merging Rfactor)
value for a dataset that I have already processed with HKL2000/Scalepack
and refined.  Is there a straightforward way to obtain this value from
my data?  From what I understand, most of my options involve going back
and obtaining unmerged intensities.  I am hoping there may be a way for
me to avoid having to backtrack that far, as this data is now very far
along in the refinement process.

Thank you,
Michelle Deaton

University of Denver
Department of Chemistry and Biochemistry