Abstract
A CONSIDERABLE problem hampering the analysis of protein crystal structures has been the damage caused to the crystals by the X-ray beam. Another limiting factor has been the resolution in the diffraction pattern. To increase the useful life of a protein crystal in the X-ray beam1, single crystal monochromators and low temperatures have been used. We now report that styrene and other vinyl monomers can decrease the radiation damage of the crystal in the X-ray beam by a factor of as much as 10, and extend the diffraction pattern so that higher angle reflections can be measured.
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References
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ZALOGA, G., SARMA, R. New method for extending the diffraction pattern from protein crystals and preventing their radiation damage. Nature 251, 551–552 (1974). https://doi.org/10.1038/251551a0
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DOI: https://doi.org/10.1038/251551a0
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