IUCrJ (Mar 2014)

Femtosecond X-ray diffraction from two-dimensional protein crystals

  • Matthias Frank,
  • David B. Carlson,
  • Mark S. Hunter,
  • Garth J. Williams,
  • Marc Messerschmidt,
  • Nadia A. Zatsepin,
  • Anton Barty,
  • W. Henry Benner,
  • Kaiqin Chu,
  • Alexander T. Graf,
  • Stefan P. Hau-Riege,
  • Richard A. Kirian,
  • Celestino Padeste,
  • Tommaso Pardini,
  • Bill Pedrini,
  • Brent Segelke,
  • M. Marvin Seibert,
  • John C. H. Spence,
  • Ching-Ju Tsai,
  • Stephen M. Lane,
  • Xiao-Dan Li,
  • Gebhard Schertler,
  • Sebastien Boutet,
  • Matthew Coleman,
  • James E. Evans

DOI
https://doi.org/10.1107/S2052252514001444
Journal volume & issue
Vol. 1, no. 2
pp. 95 – 100

Abstract

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X-ray diffraction patterns from two-dimensional (2-D) protein crystals obtained using femtosecond X-ray pulses from an X-ray free-electron laser (XFEL) are presented. To date, it has not been possible to acquire transmission X-ray diffraction patterns from individual 2-D protein crystals due to radiation damage. However, the intense and ultrafast pulses generated by an XFEL permit a new method of collecting diffraction data before the sample is destroyed. Utilizing a diffract-before-destroy approach at the Linac Coherent Light Source, Bragg diffraction was acquired to better than 8.5 Å resolution for two different 2-D protein crystal samples each less than 10 nm thick and maintained at room temperature. These proof-of-principle results show promise for structural analysis of both soluble and membrane proteins arranged as 2-D crystals without requiring cryogenic conditions or the formation of three-dimensional crystals.

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