Abstract
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.
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Acknowledgments
We thank Ian Carmichael and Kathryn Shelley for their comments on this contribution, Charles Bury and Eugenio de la Mora for making the figures, and Markus Gerstel for carrying out a survey of the PDB regarding the temperature of data collection. We also acknowledge those many colleagues with whom we have discussed the issues related to radiation damage in MX. We especially thank the ESRF for access to beamtime since 2000 under the Radiation Damage BAG, which has allowed us to carry out systematic studies on many aspects of the topic.
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Garman, E.F., Weik, M. (2017). Radiation Damage in Macromolecular Crystallography. In: Wlodawer, A., Dauter, Z., Jaskolski, M. (eds) Protein Crystallography. Methods in Molecular Biology, vol 1607. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7000-1_20
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