NIH NIGMS Mature Synchrotron Resources for Structural Biology (P30)

NIH NIGMS Mature Synchrotron Resources for Structural Biology (P30) is sponsored by National Institutes of Health (NIH). Supports mature synchrotron facilities providing X-ray beamlines and user training for structural biology research.

Mature Synchrotron Resources for Structural Biology (P30) Program | National Institute of General Medical Sciences The Mature Synchrotron Resources (MSRs) for Structural Biology (new NOFO forecast PAR-26-029 ) connect biomedical researchers with state-of-the-art X-ray beamlines, hands-on user support, and expert training to generate and analyze structural and cellular biology data.

MSRs are accessible to all biomedical researchers whose projects are vetted through a peer review process. Explore the Available MSRs below to find available techniques and learn how to request access MSRs provide assistance with data collection, processing, and analysis. This includes guidance on sample preparation and shipping, as well as support throughout the experimental process.

User access is available on an equal-opportunity, nationwide basis, with supported techniques including fiber diffraction, macromolecular crystallography, small- and wide-angle X-ray scattering, soft X-ray tomography, X-ray spectroscopy and imaging, and X-ray footprinting Training is available through on-site and remote sessions, workshops, and instructional videos.

ALS Efficiently Networking Advanced Beam Line Experiments (ALS-ENABLE) ALS-ENABLE @ ALS/Lawrence Berkeley National Laboratory Macromolecular Crystallography, Small-Angle X-ray Scattering, X-ray Footprinting with Mass Spectrometry.

X-Ray Footprinting with Mass Spectrometry SCOPER program combines deep learning with small angle X-ray scattering (SAXS) experimental data for more accurate Images courtesy of Dr. Paul Adams Biophysics Collaborative Access Team (BioCAT) BioCAT @ APS/Argonne National Laboratory Small-Angle X-ray Scattering, Fiber Diffraction An ensemble of conformational states modeled based on SAXS X-ray diffraction of muscle fiber Images courtesy of Dr. Thomas Irving Center for Biomolecular Structure at NSLS-II CBMS @ NSLS-II/Brookhaven National Laboratory Macromolecular Crystallography, Small- and Wide-Angle X-ray Automated SAXS data collection Frontier Microfocusing Macromolecular Crystallography Images courtesy of Dr. Sean McSweeney GM/CA @ APS: A Macromolecular Crystallography Resource GM/CA @ APS/Argonne National Laboratory Macromolecular Crystallography Crystal structure of the κ-opioid receptor bound to nalfurafine (salmon) and stabilized by a nanobody (cyan) 2Fo-Fc Electron density for trypsin (1.

0-Å resolution) 2Fo-Fc Electron density for crambin (0. 7-Å resolution) Images courtesy of Dr. Robert Fischetti and Dr. Janet Smith Macromolecular Diffraction Facility at the Cornell High Energy Synchrotron Source (MacCHESS) MacCHESS @ CHESS/Cornell University Macromolecular Crystallography, Small-Angle X-ray Scattering The diffuse scattering setup at FlexX. A scattering map from the Ando group at Cornell.

A central section of a 3D scattering map from the Thorne group at Cornell.

Images courtesy of Dr. Richard Cerione National Center for X-ray Tomography (NCXT) NCXT @ ALS/Lawrence Berkeley National Laboratory NE-CAT Center for Advanced Macromolecular Crystallography NE-CAT @ APS/Argonne National Laboratory Macromolecular Crystallography The structural model of a de novo designed protein that neutralizes lethal snake venom toxins Scientists at the beamline Images courtesy of Dr. Frank Murphy Structural Molecular Biology (SMB) at the Stanford Synchrotron Radiation SMB @ SSRL/SLAC National Accelerator Laboratory Macromolecular Crystallography, Small-Angle X-ray Scattering, X-ray Spectroscopy, and Imaging Surface representation of the dimeric LAG-3 protein Surface representation of the dimeric LAG-3 protein (left).

The X-ray crystal structure was solved using data collected after screening more than 3,000 crystals. The small-angle X-ray scattering (SAXS) tensor tomography image of myelin Automated and high-throughput X-ray absorption spectroscopy (XAS) for remote access use Images courtesy of Dr. Keith Hodgson Guidance on preparing and submitting annual Research Performance Progress Reports (RPPRs) is available below.

RPPR Guidance for Funded Resources Word Template [DOCX] For more information or assistance contact the program staff: This page last updated on