New Beamlines For Protein Crystallography At The EMBL-Outstation Hamburg
- EMBL-Outstation, Notkestr.85, D-22603 Hamburg (Germany)
Three new beamlines for Protein Crystallography were built up on a bending magnet fan of the DORIS III storage ring. A 10 mrad wide fan of white Synchrotron Radiation (SR) is evenly distributed among 3 individual stations: X12, a central, wavelength-tunable station intended for anomalous scattering experiments (MAD) and fixed wavelength, high intensity stations symmetrically on either side. The fixed wavelength beamlines X11 and X13 comprise triangular, asymmetrically cut Si (111) monochromators as horizontally focusing optical elements. The tunable station is based on a fixed-exit, horizontally focusing double crystal monochromator system. Vertical focusing is achieved on all three lines by trapezoidal shaped, continuous Rh-coated mirrors which can be dynamically bent. In all three lines the X-ray beam can be examined at various points on its way through the optical system by removable screens and PIN-diode based intensity monitors. Purpose built crystallographic end-stations complete the set-up. The design of individual components and their performance will be described.
- OSTI ID:
- 20652960
- Journal Information:
- AIP Conference Proceedings, Vol. 705, Issue 1; Conference: 8. international conference on synchrotron radiation instrumentation, San Francisco, CA (United States), 25-29 Aug 2003; Other Information: DOI: 10.1063/1.1757814; (c) 2004 American Institute of Physics; Country of input: International Atomic Energy Agency (IAEA); ISSN 0094-243X
- Country of Publication:
- United States
- Language:
- English
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