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Previous proof-of-concept measurements on single-layer two-dimensional membrane-protein crystals performed at X-ray free-electron lasers (FELs) have demonstrated that the collection of meaningful diffraction patterns, which is not possible at synchrotrons because

Previous proof-of-concept measurements on single-layer two-dimensional membrane-protein crystals performed at X-ray free-electron lasers (FELs) have demonstrated that the collection of meaningful diffraction patterns, which is not possible at synchrotrons because of radiation-damage issues, is feasible. Here, the results obtained from the analysis of a thousand single-shot, room-temperature X-ray FEL diffraction images from two-dimensional crystals of a bacteriorhodopsin mutant are reported in detail.

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    Date Created
    • 2018-01
    Resource Type
  • Text
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    Identifier
    • Digital object identifier: 10.1107/S2052252517017043
    • Identifier Type
      International standard serial number
      Identifier Value
      2052-2525

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    Casadei, C. M., Tsai, C., Barty, A., Hunter, M. S., Zatsepin, N. A., Padeste, C., . . . Frank, M. (2018). Resolution extension by image summing in serial femtosecond crystallography of two-dimensional membrane-protein crystals. IUCrJ, 5(1), 103-117. doi:10.1107/s2052252517017043

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