Abstract

The National Synchrotron Light Source (NSLS) at Brookhaven National Laboratory (BNL) is a user facility devoted to research that uses infrared, visible, ultraviolet, and Xradiation. Eight x-ray beamlines are used regularly for macromolecular and virus crystallography, one is being commissioned, and one more is being developed. This Research Resource ties together five of the eight operating beamlines to enhance the capabilities of the NSLS in PX through innovation in software and methods and continued beamline development. This proposal includes both new initiatives and continuation of projects from the previous cycle of this grant. There will be commissioning of a new undulator-based beamline, and improvement of a wiggler beamline to an undulator source. We have developed an innovative program to support mail-in data collection service. We are preparing to install robotic specimen-mounting apparatus. We continue to improve our methods and software for remote, conventional, and automated operations. And we continue studies on the usefulness of exotic crystallographic methods such as multi-beam diffraction. This resource has helped to continue the role of the NSLS as a center for structural biology in the northeastern United States. The Resource represents an extension of the close cooperation that exists between the BNL Biology Department and the NSLS.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR012408-07
Application #
6669365
Study Section
Special Emphasis Panel (ZRG1-PC (02))
Program Officer
Swain, Amy L
Project Start
1998-09-30
Project End
2008-06-30
Budget Start
2003-09-15
Budget End
2004-06-30
Support Year
7
Fiscal Year
2003
Total Cost
$2,461,651
Indirect Cost

  Institution

Name
Brookhaven National Laboratory
Department
Type
DUNS #
027579460
City
Upton
State
NY
Country
United States
Zip Code
11973

  Publications

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
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
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
Tajima, Nami; Karakas, Erkan; Grant, Timothy et al. (2016) Activation of NMDA receptors and the mechanism of inhibition by ifenprodil. Nature 534:63-8
Ericson, Daniel L; Yin, Xingyu; Scalia, Alexander et al. (2016) Acoustic Methods to Monitor Protein Crystallization and to Detect Protein Crystals in Suspensions of Agarose and Lipidic Cubic Phase. J Lab Autom 21:107-14

Showing the most recent 10 out of 167 publications