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. The general area of research in our laboratory involves the biochemistry, enzymology and structural biology of bacterial enzymes implicated in antibiotic resistance, primarily those enzymes responsible for the deactivation of beta-lactam and aminoglycoside antibiotics. This proposal for beam time at SSRL focuses on the collection of high resolution diffraction data on native and mutant enzymes, and substrate/inhibitor complexes. The desire to collect data at SSRL is based upon our need for high quality, high resolution diffraction data from a number of different crystals, some of which diffract to atomic resolution, particularly in the case of the beta-lactamase enzymes. In addition, we are now producing the majority of our proteins as seleno-methionine derivatives, and we envisage an increased requirement for the collection of accurate MAD data.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR001209-31
Application #
8170303
Study Section
Special Emphasis Panel (ZRG1-BCMB-P (40))
Project Start
2010-05-01
Project End
2011-02-28
Budget Start
2010-05-01
Budget End
2011-02-28
Support Year
31
Fiscal Year
2010
Total Cost
$346
Indirect Cost
Name
Stanford University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
009214214
City
Stanford
State
CA
Country
United States
Zip Code
94305
Aleman, Fernando; Tzarum, Netanel; Kong, Leopold et al. (2018) Immunogenetic and structural analysis of a class of HCV broadly neutralizing antibodies and their precursors. Proc Natl Acad Sci U S A 115:7569-7574
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