Matching X-ray source, optics and detectors to protein crystallography requirements.
A review of the requirements for collecting X-ray diffraction data from protein crystals is given, with an emphasis on the properties of the crystal and its diffraction pattern. The size, unit-cell dimensions and perfection of the crystals can all be related to the required size and divergence of the incident X-ray beam, together with the size and spatial resolution of the detector. The X-ray beam causes primary radiation damage, even in frozen crystals. If the incident beam is very intense, temperature rises and gradients could occur in the crystal. The extent to which these problems can be overcome is also discussed.
Nave
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CCLRC Daresbury Laboratory, Daresbury Warrington WA4 4AD, England. c.nave@dl.ac.uk
D003460:Crystallization; D018360:Crystallography, X-Ray / Q000295:instrumentation / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D017356:Synchrotrons
D011506:Proteins