This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. This proposal covers two projects involving studies of protein-ligand interactions. The first is a continuing search for well-ordered crystals of rhodopsin and its complexes with other signaling proteins. How G protein-coupled receptors respond to their environment and interact with G proteins to create intracellular signals is not understood at the molecular structure level. We are attempting to crystallize complexes relevant to the signaling process and want to use synchrotron radiation to determine their structures. Our current crystals are small and poorly-ordered. How well they diffract would be difficult to determine without access to synchrotron sources. Our second project involves obtaining high or ultra-high resolution diffraction data for streptavidin mutants and their biotin complexes. We want to compare molecular dynamics simulations and anisotropic atomic displacement parameters to better understand the dynamics of protein/small molecule (drug?) interactions. We currently have several high-resolution data sets for the comparison, but we anticipate expanding our studies to include additional mutants.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-32
Application #
8362165
Study Section
Special Emphasis Panel (ZRG1-BCMB-P (40))
Project Start
2011-03-01
Project End
2012-02-29
Budget Start
2011-03-01
Budget End
2012-02-29
Support Year
32
Fiscal Year
2011
Total Cost
$279
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
Batyuk, Alexander; Galli, Lorenzo; Ishchenko, Andrii et al. (2016) Native phasing of x-ray free-electron laser data for a G protein-coupled receptor. Sci Adv 2:e1600292
Lins, Brittney R; Pushie, Jake M; Jones, Michael et al. (2016) Mapping Alterations to the Endogenous Elemental Distribution within the Lateral Ventricles and Choroid Plexus in Brain Disorders Using X-Ray Fluorescence Imaging. PLoS One 11:e0158152
Sierra, Raymond G; Gati, Cornelius; Laksmono, Hartawan et al. (2016) Concentric-flow electrokinetic injector enables serial crystallography of ribosome and photosystem II. Nat Methods 13:59-62
Cowley, Ryan E; Cirera, Jordi; Qayyum, Munzarin F et al. (2016) Structure of the Reduced Copper Active Site in Preprocessed Galactose Oxidase: Ligand Tuning for One-Electron O2 Activation in Cofactor Biogenesis. J Am Chem Soc 138:13219-13229
Edlund, Petra; Takala, Heikki; Claesson, Elin et al. (2016) The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography. Sci Rep 6:35279
McLuskey, Karen; Grewal, Jaspreet S; Das, Debanu et al. (2016) Crystal Structure and Activity Studies of the C11 Cysteine Peptidase from Parabacteroides merdae in the Human Gut Microbiome. J Biol Chem 291:9482-91
Colletier, Jacques-Philippe; Sawaya, Michael R; Gingery, Mari et al. (2016) De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure. Nature 539:43-47
Agrawal, Anant A; Salsi, Enea; Chatrikhi, Rakesh et al. (2016) An extended U2AF(65)-RNA-binding domain recognizes the 3' splice site signal. Nat Commun 7:10950
Kaever, Thomas; Matho, Michael H; Meng, Xiangzhi et al. (2016) Linear Epitopes in Vaccinia Virus A27 Are Targets of Protective Antibodies Induced by Vaccination against Smallpox. J Virol 90:4334-45
Nogly, Przemyslaw; Panneels, Valerie; Nelson, Garrett et al. (2016) Lipidic cubic phase injector is a viable crystal delivery system for time-resolved serial crystallography. Nat Commun 7:12314

Showing the most recent 10 out of 563 publications