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

Publiceringsår: 2004
Språk: Engelska
Sidor: 808-811
Publikation/Tidskrift/Serie: AIP Conference Proceedings
Volym: 705
Nummer: 1
Dokumenttyp: Konferensbidrag
Förlag: American Institute of Physics


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


  • Physical Sciences
  • Natural Sciences
  • Biological Sciences


SYNCHROTRON RADIATION INSTRUMENTATION: Eighth International Conference on Synchrotron Radiation Instrumentation
  • ISBN: 0-7354-0179-9

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