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Radiation damage inflicted on macromolecular crystals during X-ray diffraction experiments remains a limiting factor for structure solution, even when samples are cooled to cryotemperatures (~100 K). Efforts to establish mitigation strategies are ongoing and various approaches, summarized below, have been investigated over the last 15 years, resulting in a deeper understanding of the physical and chemical factors affecting damage rates. The recent advent of X-ray free electron lasers permits "diffraction-before-destruction" by providing highly brilliant and short (a few tens of fs) X-ray pulses. New fourth generation synchrotron sources now coming on line with higher X-ray flux densities than those available from third generation synchrotrons will bring the issue of radiation damage once more to the fore for structural biologists.

Original publication




Journal article


Methods Mol Biol

Publication Date





467 - 489


Absorbed dose, Cryocrystallography, Global and specific radiation damage, Radiation damage mitigation, Radicals and their scavengers, X-ray-matter interactions, Crystallization, Crystallography, X-Ray, Electrons, Free Radical Scavengers, Free Radicals, Lasers, Macromolecular Substances, Protein Conformation, Proteins, Radiation Dosage, Synchrotrons, X-Rays