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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

DOI

10.1007/978-1-4939-7000-1_20

Type

Journal article

Journal

Methods Mol Biol

Publication Date

2017

Volume

1607

Pages

467 - 489

Keywords

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