The Macromolecular Crystallography Research Resource (PXRR) at the National Synchrotron Light Source (NSLS) operates six beamlines that are employed for research by about 160 outside research groups and half a dozen Brookhaven Lab groups. These scientists produce over 200 research publications in a typical year, and over 300 Protein Data Bank depositions in the past year. The PXRR have pioneered an active Mail-in program that involves ongoing collaborations with about 15 outside research groups and short collaborations or service projects with many more. The Mail-in program has interacted with 90 groups in the past several years;each year for the past four years there have been about 25 PDB depositions and 15 publications from the Mail-in program. The PXRR performs research and development on apparatus, methods, and software to improve the technology for synchrotron-based macromolecular crystallography. Special emphases during the coming cycle will be on the development of detectors that will match the power and collimation of modern x-ray sources, the use of micron-sized crystals, the development of robotic cryogenic specimen handling, and the simultaneous measurement of UV, Visible, or Raman IR spectra with x-ray diffraction. The PXRR staff will execute numerous small research programs, among other things to improve visualization of tiny specimens and improve cryogenic preservation of specimens. A long-term goal for the PXRR is to create a resource for macromolecular crystallography at NSLS-II, the new synchrotron light source that is being created at Brookhaven Lab during the next five to seven years. The objective will be to have several macromolecular crystallography beamlines in operation when NSLS-II begins operation. This project will involve direct cooperation with NSLS-II staff to develop a complete plan for such facilities, and then to begin to achieve that plan.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR012408-15
Application #
8122268
Study Section
Special Emphasis Panel (ZRG1-BCMB-R (40))
Program Officer
Swain, Amy L
Project Start
1998-10-02
Project End
2013-06-30
Budget Start
2011-07-01
Budget End
2012-06-30
Support Year
15
Fiscal Year
2011
Total Cost
$2,458,172
Indirect Cost
Name
Brookhaven National Laboratory
Department
Type
DUNS #
027579460
City
Upton
State
NY
Country
United States
Zip Code
11973
Sui, Xuewu; Farquhar, Erik R; Hill, Hannah E et al. (2018) Preparation and characterization of metal-substituted carotenoid cleavage oxygenases. J Biol Inorg Chem 23:887-901
Jacques, Benoit; Coinçon, Mathieu; Sygusch, Jurgen (2018) Active site remodeling during the catalytic cycle in metal-dependent fructose-1,6-bisphosphate aldolases. J Biol Chem 293:7737-7753
Fuller, Franklin D; Gul, Sheraz; Chatterjee, Ruchira et al. (2017) Drop-on-demand sample delivery for studying biocatalysts in action at X-ray free-electron lasers. Nat Methods 14:443-449
Wangkanont, Kittikhun; Winton, Valerie J; Forest, Katrina T et al. (2017) Conformational Control of UDP-Galactopyranose Mutase Inhibition. Biochemistry 56:3983-3992
VanderLinden, Ryan T; Hemmis, Casey W; Yao, Tingting et al. (2017) Structure and energetics of pairwise interactions between proteasome subunits RPN2, RPN13, and ubiquitin clarify a substrate recruitment mechanism. J Biol Chem 292:9493-9504
Song, Lingshuang; Yang, Lin; Meng, Jie et al. (2017) Thermodynamics of Hydrophobic Amino Acids in Solution: A Combined Experimental-Computational Study. J Phys Chem Lett 8:347-351
Orlova, Natalia; Gerding, Matthew; Ivashkiv, Olha et al. (2017) The replication initiator of the cholera pathogen's second chromosome shows structural similarity to plasmid initiators. Nucleic Acids Res 45:3724-3737
Firestone, Ross S; Cameron, Scott A; Karp, Jerome M et al. (2017) Heat Capacity Changes for Transition-State Analogue Binding and Catalysis with Human 5'-Methylthioadenosine Phosphorylase. ACS Chem Biol 12:464-473
Arturo, Emilia C; Gupta, Kushol; Héroux, Annie et al. (2016) First structure of full-length mammalian phenylalanine hydroxylase reveals the architecture of an autoinhibited tetramer. Proc Natl Acad Sci U S A 113:2394-9
McMillan, Brian J; Tibbe, Christine; Jeon, Hyesung et al. (2016) Electrostatic Interactions between Elongated Monomers Drive Filamentation of Drosophila Shrub, a Metazoan ESCRT-III Protein. Cell Rep 16:1211-1217

Showing the most recent 10 out of 167 publications