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The introduction of highly intense wiggler and undulator beamlines has reintroduced the problem of X-ray radiation damage in protein crystals even at cryogenic temperatures. Several metrics for monitoring radiation damage are considered and unit-cell volume expansion is systematically investigated using crystals of three different types, but it is found to be too variable to be a useful metric. Radical scavengers of secondary radiation damage are investigated as possible mitigating agents. Styrene is found to be ineffective. A method of spectroscopically measuring the radiation damage with a microspectrophotometer was used and, in conjunction with crystallographic data, provided tentative but suggestive evidence for the efficacy of ascorbate as a free-radical scavenging agent in cryocooled hen egg-white lysozyme crystals.

Original publication




Journal article


J Synchrotron Radiat

Publication Date





347 - 354


Animals, Crystallography, X-Ray, Egg Proteins, Free Radical Scavengers, Humans, Metronidazole, Muramidase, Protein Conformation, Radiation Injuries, X-Ray Diffraction