Description
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

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.
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    Title
    • Serial crystallography at synchrotrons and X-ray lasers
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    Date Created
    2017-03
    Resource Type
  • Text
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    Identifier
    • Digital object identifier: 10.1107/S2052252517001877
    • Identifier Type
      International standard serial number
      Identifier Value
      2052-2525
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    • View the article as published at http://journals.iucr.org/m/issues/2017/02/00/me0641/index.html

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    Standfuss, J., & Spence, J. (2017). Serial crystallography at synchrotrons and X-ray lasers. IUCrJ, 4(2), 100-101. doi:10.1107/s2052252517001877

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