SIBYLS — a SAXS and Protein Crystallography Beamline at the ALS

AIP CONFERENCE PROCEEDINGS(2004)

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摘要
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 Testa 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/DeltaEsimilar to1/110). Flux rates with Si(111) crystals for PX are measured as 2x10(11) hv/sec through a 100mum pinhole at 12.4KeV. For SAXS the flux is up to 3x10(13) photons/sec at 10KeV with all apertures open when using the multilayer monochromator elements. The performance characteristics of this unique beamline will be described.
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apertures,performance,proteins,scattering,gamma ray,particle accelerators,x ray spectroscopy,particle acceleration,high resolution,resolution,biology,dipoles,protein crystallography,small angle x ray scattering,engineering,synchrotron radiation,data collection,small angle scattering,crystallography
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