X-ray crystallography is a basic technique to study structure and function of bio-macromolecules. Single/multiple anomalous dispersion (SAD/MAD) has become the method of choice for determining novel crystal structures by X-ray crystallography, due to the increasing availability of synchrotron radiation sources in the past 10 years. SAD/MAD requires X-ray diffraction measurements at one or two to four X-ray energies near an atomic absorption edge of a heavy atom (i.e. Se, Fe, Cu, Br, Tb, Pt, Hg, W, Au, and Zn). The broad band tunability of synchrotron radiation sources allows X-ray data collection at multiple wavelengths for highly efficient structure determination. Case Proteomics Center and Case Synchrotron for Synchrotron Biosciences manages two beamlines (X29 and X3A) at the National Synchrotron Light Source for macromolecular crystallography, with X29 being the most active and oversubscribed crystallography beamline on the east coast and the fourth largest contributor of all synchrotron beamlines worldwide to the Protein Databank (PDB) since 2007.
For more information on the X29 Beamline or the X3A Beamline, click X29 or X3A.
Contact Person:
Wuxian Shi, Ph.D. (wushi@bnl.gov)
National Synchrotron Light Source
Bldg. 725A-X29
Brookhaven National Laboratory
Upton, NY 11973
Office Location: Building 535, Room 1-A108
Phone: (631) 344-2099
Fax: (631) 344-5594