Femtosecond X-ray diffraction from two-dimensional protein crystals

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

Research output: Contribution to journalArticlepeer-review

68 Scopus citations


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 8.5Å resolution for two different 2-D protein crystal samples each less than 10nm 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.

Original languageEnglish (US)
Pages (from-to)95-100
Number of pages6
StatePublished - Feb 28 2014


  • femtosecond crystallography
  • membrane protein
  • single layer X-ray diffraction
  • two-dimensional protein crystal

ASJC Scopus subject areas

  • Chemistry(all)
  • Biochemistry
  • Materials Science(all)
  • Condensed Matter Physics


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