Current Status of Crystallography Beamlines and End Stations at NSRRC

摘要

Protein crystallography is one of the most powerful and dominant tools to determine the three-dimensional structures of biological macromolecules today. In order to increase the rate of crystal structure determination, the highly brilliant and easily tunable synchrotron radiation (SR) X-ray source is essential to meet the needs of abound structural information for studying structural genomics and structural-based drug designs. To satisfy these requirements, the National Synchrotron Radiation Research Center (NSRRC) has constructed two dedicated Synchrotron Radiation Protein Crystallography Facility (SPXF) high-throughput beamlines for structural genomics research. One of the beamlines will be a multi-wavelength anomalous diffraction (MAD) beamline with energy tunability from 6.5 keV to 19 keV for unknown structure determinations, and the other will be a monochromatic (mono) beamline with energy from 12 keV to 14 keV for crystal screening, drug design and high-resolution structure studies. The well-developed light source technique, advanced area detectors, high-efficient computing and network environments, automatic crystal sample changing and centering, and user-friendly data collection and control systems will produce 800 MAD data set per year for MAD beamline and 1200 useful data sets per year for mono beamline.