| Literature DB >> 28628129 |
Philip Roedig1, Helen M Ginn2,3, Tim Pakendorf1, Geoff Sutton2, Karl Harlos2, Thomas S Walter2, Jan Meyer1, Pontus Fischer1, Ramona Duman3, Ismo Vartiainen4, Bernd Reime1, Martin Warmer1, Aaron S Brewster5, Iris D Young5, Tara Michels-Clark5, Nicholas K Sauter5, Abhay Kotecha2, James Kelly6,7, David J Rowlands6, Marcin Sikorsky8, Silke Nelson8, Daniel S Damiani8, Roberto Alonso-Mori8, Jingshan Ren2, Elizabeth E Fry2, Christian David9, David I Stuart2,3, Armin Wagner3, Alke Meents1,10.
Abstract
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.Entities:
Mesh:
Year: 2017 PMID: 28628129 PMCID: PMC5588887 DOI: 10.1038/nmeth.4335
Source DB: PubMed Journal: Nat Methods ISSN: 1548-7091 Impact factor: 28.547