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Open Access Publications from the University of California

SIBYLS - A SAXS and protein crystallography beamline at the ALS

  • Author(s): Trame, Christine
  • MacDowell, Alastair A.
  • Celestre, Richard S.
  • Padmore, Howard A.
  • Cambie, Daniella
  • Domning, Edward E.
  • Duarte, Robert M.
  • Kelez, Nicholas
  • Plate, David W.
  • Holton, James M.
  • Frankel, Kenneth
  • Tsutakawa, Susan
  • Tsuruta, Hiro
  • Tainer, John A.
  • Cooper, Priscilla K.
  • et al.

The new Structurally Integrated BiologY for Life Sciences (SIBYLS) beamline at the Advanced Light Source will be dedicated to Macromolecular Crystallography (PX) and Small Angle X-ray Scattering (SAXS). SAXS will provide structural information of macromolecules in solutions and will complement high resolution PX studies on the same systems but in a crystalline state. The x-ray source is one of the 5 Tesla superbend dipoles recently installed at the ALS that allows for a hard x-ray program to be developed on the relatively low energy Advanced Light Source (ALS) ring (1.9 GeV). The beamline is equipped with fast interchangeable monochromator elements, consisting of either a pair of single Si(111) crystals for crystallography, or a pair of multilayers for the SAXS mode data collection (E/ΔE~;1/110). Flux rates with Si(111) crystals for PX are measured as 2x1011 hv/sec/400 mA through a 100μm pinhole at 12.4 KeV. For SAXS the flux is up to 3x1013 photons/sec/400 mA at 10 KeV with all apertures open when using the multilayer monochromator elements. The performance characteristics of this unique beamline will be described.

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