[ccp4bb] Five Postdoctoral Positions at Oak Ridge National Laboratory
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
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
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
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