This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Biology Department of BNL is a member of the NYSGXRC funded by the National Institutes of Health under their Protein Structure Initiative (PSI) program. The goal of the PSI is to provide structural information for virtually all naturally occurring protein sequences using a combination of experimental and structure modeling techniques. The NYSGXRC uses X-ray crystallography for structure determination and MODELER for modeling homologous proteins of the same family. Many of the target selection strategies of the NYSGXRC are biologically based, providing a set of proteins that are related and representative of a larger set of proteins in some fashion. The strategies include: all members of an enzymatic pathway, each protein in macromolecular complex, interacting partners of related proteins identified using 2-hybrid screening or bioinformatics analysis, or a group of gene products up and down-regulated in a biological process as determined by DNA-microarray techniques, or a group of proteins of unknown function and structure but known to be important for the survival of H. influenzae.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR012408-10
Application #
7358892
Study Section
Special Emphasis Panel (ZRG1-PC (02))
Project Start
2006-07-01
Project End
2007-06-30
Budget Start
2006-07-01
Budget End
2007-06-30
Support Year
10
Fiscal Year
2006
Total Cost
$60,649
Indirect Cost
Name
Brookhaven National Laboratory
Department
Type
DUNS #
027579460
City
Upton
State
NY
Country
United States
Zip Code
11973
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
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