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Bent Diamond Crystals and Multilayer Based Optics at the new 5-Station Protein Crystallography Beamline ‘Cassiopeia’ at MAX-lab

Author

Summary, in English

A new 5-station beamline for protein crystallography is being commissioned at the Swedish synchrotron light source MAX-II at Lund University. Of the 2K/gamma = 14 mrad horizontal wiggler fan, the central 2 mrad are used and split in three parts. The central 1 mrad will be used for a station optimized for MAD experiments and on each side of the central fan, from 0.5 mrad to 1 mrad, there are two fixed energy stations using different energies of the same part of the beam. These, in total five stations, can be used simultaneously and independently for diffraction data collection. The two upstream monochromators for the side stations are meridionally bent asymmetric diamond(111) crystals in Laue transmission geometry. The monochromators for the downstream side stations are bent Ge(111) crystals in asymmetric Bragg reflection geometry. Curved multilayer mirrors inserted in the monochromatic beams provide focusing in the vertical plane. The first side station is under commissioning, and a preliminary test protein data set has been collected. ©2004 American Institute of Physics

Publishing year

2004

Language

English

Pages

808-811

Publication/Series

AIP Conference Proceedings

Volume

705

Issue

1

Document type

Conference paper

Publisher

American Institute of Physics (AIP)

Topic

  • Physical Sciences
  • Natural Sciences
  • Biological Sciences

Conference name

SYNCHROTRON RADIATION INSTRUMENTATION: Eighth International Conference on Synchrotron Radiation Instrumentation

Conference date

2003-08-25 - 2003-08-29

Status

Published

ISBN/ISSN/Other

  • ISBN: 0-7354-0179-9