Femtosecond X-ray diffraction from two-dimensional protein crystals

نویسندگان

  • 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
چکیده

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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عنوان ژورنال:

دوره 1  شماره 

صفحات  -

تاریخ انتشار 2014