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High-speed fixed-target serial virus crystallography

  • Author(s): Roedig, P
  • Ginn, HM
  • Pakendorf, T
  • Sutton, G
  • Harlos, K
  • Walter, TS
  • Meyer, J
  • Fischer, P
  • Duman, R
  • Vartiainen, I
  • Reime, B
  • Warmer, M
  • Brewster, AS
  • Young, ID
  • Michels-Clark, T
  • Sauter, NK
  • Kotecha, A
  • Kelly, J
  • Rowlands, DJ
  • Sikorsky, M
  • Nelson, S
  • Damiani, DS
  • Alonso-Mori, R
  • Ren, J
  • Fry, EE
  • David, C
  • Stuart, DI
  • Wagner, A
  • Meents, A
  • et al.
Abstract

© 2017 Nature America, Inc., part of Springer Nature. All rights reserved. We report a method for serial X-ray crystallography at X-ray free-electron lasers (XFELs), which allows for full use of the current 120-Hz repetition rate of the Linear Coherent Light Source (LCLS). Using a micropatterned silicon chip in combination with the high-speed Roadrunner goniometer for sample delivery, we were able to determine the crystal structures of the picornavirus bovine enterovirus 2 (BEV2) and the cytoplasmic polyhedrosis virus type 18 polyhedrin, with total data collection times of less than 14 and 10 min, respectively. Our method requires only micrograms of sample and should therefore broaden the applicability of serial femtosecond crystallography to challenging projects for which only limited sample amounts are available. By synchronizing the sample exchange to the XFEL repetition rate, our method allows for most efficient use of the limited beam time available at XFELs and should enable a substantial increase in sample throughput at these facilities.

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