Synchrotron radiation (SR) is an extremely bright and tunable x-ray source that enables forefront research in structural molecular biology (SMB). A ?Synchrotron Structural Biology Resource is proposed for continuing support at the Stanford Synchrotron Radiation Lightsource (SSRL) by the NIH NIGMS and DOE BER to develop new technologies in macromolecular crystallography, x-ray absorption/emission spectroscopy and small angle x-ray scattering/diffraction, to train/support users, and to disseminate the newly developed capabilities to the biomedical research community. This proposal is for the continued funding, operation and future development of this SMB Resource. New initiatives will capitalize on the increasing SR performance of SSRL?s 3rd generation storage ring SPEAR3. Proposed also is the development of selected SMB applications of LCLS. A principal aim is to optimize experimental facilities and instrumentation, detectors, software and compute performance on the SMB Resource?s 9+ beam lines at SSRL (with another two in construction) to take full advantage of the high brightness provided by SPEAR3 at 500 mA current and provide innovative new instrumentation and methodologies. This will enable the SMB Resource to advance the scientific forefront with new initiatives built upon state-of-the-art instrumentation and methodologies, innovative software and automated/high-throughput systems for: studying high resolution structures/function of large, complex biomolecules and molecular machines; investigating fundamental questions in biophysics such as protein folding; and developing/improving methods for studying very fast time-resolved structural changes in chemical and biological systems with ultrafast or fast scattering and spectroscopy techniques. These scientific advancements will be facilitated by parallel developments in software to provide expanded capabilities for instrument and detector control, remote data collection and real-time data analysis. Driving biomedical projects and collaborative research and service programs involving a large number of outside scientists will drive and support core technological developments.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Biotechnology Resource Grants (P41)
Project #
5P41GM103393-38
Application #
9233143
Study Section
Special Emphasis Panel (ZRG1-BCMB-P)
Project Start
Project End
Budget Start
2017-03-01
Budget End
2018-02-28
Support Year
38
Fiscal Year
2017
Total Cost
$413,574
Indirect Cost
$113,121
Name
Stanford University
Department
Type
Domestic Higher Education
DUNS #
009214214
City
Stanford
State
CA
Country
United States
Zip Code
94304
Bitra, Aruna; Doukov, Tzanko; Wang, Jing et al. (2018) Crystal structure of murine 4-1BB and its interaction with 4-1BBL support a role for galectin-9 in 4-1BB signaling. J Biol Chem 293:1317-1329
Chiang, Linus; Wasinger, Erik C; Shimazaki, Yuichi et al. (2018) Electronic Structure and Reactivity Studies of a Nonsymmetric One-Electron Oxidized CuII Bis-phenoxide Complex. Inorganica Chim Acta 481:151-158
Moon, Thomas M; Sheehe, Jessica L; Nukareddy, Praveena et al. (2018) An N-terminally truncated form of cyclic GMP-dependent protein kinase I? (PKG I?) is monomeric and autoinhibited and provides a model for activation. J Biol Chem 293:7916-7929
Sharma, Pankaj; Maklashina, Elena; Cecchini, Gary et al. (2018) Crystal structure of an assembly intermediate of respiratory Complex II. Nat Commun 9:274
Laursen, Nick S; Friesen, Robert H E; Zhu, Xueyong et al. (2018) Universal protection against influenza infection by a multidomain antibody to influenza hemagglutinin. Science 362:598-602
Chen, Qiang; Xu, Yan; Tang, Pei (2018) X-Ray Crystallographic Studies for Revealing Binding Sites of General Anesthetics in Pentameric Ligand-Gated Ion Channels. Methods Enzymol 603:21-47
Matho, Michael H; Schlossman, Andrew; Gilchuk, Iuliia M et al. (2018) Structure-function characterization of three human antibodies targeting the vaccinia virus adhesion molecule D8. J Biol Chem 293:390-401
(2018) Retraction: Site?specific recombination of nitrogen?fixation genes in cyanobacteria by XisF–XisH–XisI complex: Structures and models, William C. Hwang, James W. Golden, Jaime Pascual, Dong Xu, Anton Cheltsov, Adam Godzik Proteins 86:268
Mirts, Evan N; Petrik, Igor D; Hosseinzadeh, Parisa et al. (2018) A designed heme-[4Fe-4S] metalloenzyme catalyzes sulfite reduction like the native enzyme. Science 361:1098-1101
Zhou, Ang; Crossland, Patrick M; Draksharapu, Apparao et al. (2018) Oxoiron(IV) complexes as synthons for the assembly of heterobimetallic centers such as the Fe/Mn active site of Class Ic ribonucleotide reductases. J Biol Inorg Chem 23:155-165

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