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Matching X-ray beam and detector properties to protein crystals of different perfection

DOI: 10.1107/S1600577514003609 DOI Help
PMID: 24763643 PMID Help

Authors: Colin Nave (Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Synchrotron Radiation , VOL 21 , PAGES 537 - 546

State: Published (Approved)
Published: May 2014

Open Access Open Access

Abstract: An analysis is given of the effect of different beam and detector parameters on the sharpness of recorded diffraction features for macromolecular crystals of different quality. The crystal quality parameters include crystal strain, crystal or mosaic block size and mosaic block misorientation. Calculations are given for instrument parameters such as angular resolution of the detector, beam divergence and wavelength bandpass to be matched to the intrinsic diffraction properties from these crystals with the aim of obtaining the best possible data out of each crystal. Examples are given using typical crystal imperfections obtained from the literature for both room-temperature and cryo-cooled crystals. Possible implications for the choice of X-ray source, beamline design, detector specifications, instrument set-up and data processing are discussed, together with the limitations of the approach.

Journal Keywords: Crystal Perfection; Synchrotron Beam Properties; Detectors; Beams; Crystals; Data Processing; Defects; Diffraction; Proteins; Synchrotrons; Temperature Range 0273-0400 K; X Radiation; X-Ray Sources

Subject Areas: Technique Development, Physics

Technical Areas: Detectors

Added On: 30/06/2014 12:17


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