Abstract
Radiation damage to the sample is one of the major sources of error in collecting accurate diffraction data in protein crystallography. However, very few systematic studies of radiation damage have been carried out and no theory which can adequately explain the susceptibility of protein crystals to various X-ray wavelengths is available. In this article a description is given of the physical, chemical and mechanical processes which could occur during protein crystallography data collection. The way radiation damage could vary with the wavelength and intensity of the indicident radiation is described and possible ways of mitigating radiation damage are discussed.
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