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130307 https://hdl.handle.net/2286/R.I.44418 Standfuss, J., & Spence, J. (2017). Serial crystallography at synchrotrons and X-ray lasers. IUCrJ, 4(2), 100-101. doi:10.1107/s2052252517001877 10.1107/S2052252517001877 2052-2525 http://rightsstatements.org/vocab/InC/1.0/ http://creativecommons.org/licenses/by/4.0 2017-03 2 pages eng Standfuss, Jorg Spence, John College of Liberal Arts and Sciences Department of Physics View the article as published at http://journals.iucr.org/m/issues/2017/02/00/me0641/index.html Recently we have seen rapid progress in the serial crystallography (SC) method at X-ray free-electron lasers (XFELs). Injection of thousands of protein microcrystals into the ∼10[superscript 12] photons of few-femtosecond XFEL pulses has allowed the structure determination of crystals grown in vivo, or of submicron size, and from challenging targets such as membrane proteins. For time-resolved studies, the small crystal size allows for rapid diffusive saturation in mix-and-inject analysis of biochemical reactions, and full optical saturation of the sample by a pump laser in studies of light-driven proteins. The ability to outrun most radiation damage avoids the need for sample cooling and its artifacts, allowing studies of molecular machines at work in their correct room-temperature thermal bath or a controlled chemical environment. Text Serial crystallography at synchrotrons and X-ray lasers