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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 of radiation-damage issues, is feasible. Here, the results obtained from

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. The high redundancy in the measurements boosts the intensity signal-to-noise ratio, so that the values of the diffracted intensities can be reliably determined down to the detector-edge resolution of 4 Å. The results show that two-dimensional serial crystallography at X-ray FELs is a suitable method to study membrane proteins to near-atomic length scales at ambient temperature. The method presented here can be extended to pump–probe studies of optically triggered structural changes on submillisecond timescales in two-dimensional crystals, which allow functionally relevant large-scale motions that may be quenched in three-dimensional crystals.

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    Title
    • Resolution Extension by Image Summing in Serial Femtosecond Crystallography of Two-Dimensional Membrane-Protein Crystals
    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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    • View the article as published at http://journals.iucr.org/m/issues/2018/01/00/ec5006/index.html

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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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