Femtosecond X-ray diffraction from two-dimensional protein crystals Academic Article uri icon

abstract

  • 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.

authors

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

publication date

  • 2014

published in