Journal Article PUBDB-2015-01262

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Fixed-Target Protein Serial Microcrystallography with an X-ray Free Electron Laser

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2014
Nature Publishing Group London

Scientific reports 4(6026), 1 () [10.1038/srep06026]
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Abstract: We present results from experiments at the Linac Coherent Light Source (LCLS) demonstrating that serial femtosecond crystallography (SFX) can be performed to high resolution (~2.5 Å) using protein microcrystals deposited on an ultra-thin silicon nitride membrane and embedded in a preservation medium at room temperature. Data can be acquired at a high acquisition rate using x-ray free electron laser sources to overcome radiation damage, while sample consumption is dramatically reduced compared to flowing jet methods. We achieved a peak data acquisition rate of 10 Hz with a hit rate of ~38%, indicating that a complete data set could be acquired in about one 12-hour LCLS shift using the setup described here, or in even less time using hardware optimized for fixed target SFX. This demonstration opens the door to ultra low sample consumption SFX using the technique of diffraction-before-destruction on proteins that exist in only small quantities and/or do not produce the copious quantities of microcrystals required for flowing jet methods.

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Note: OA

Contributing Institute(s):
  1. CFEL-Coherent X-Ray Imaging (FS-CFEL-1)
Research Program(s):
  1. Experiments at CFEL (POF2-544) (POF2-544)
Experiment(s):
  1. Experiments at CFEL

Appears in the scientific report 2014
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Medline ; Creative Commons Attribution-NonCommercial-NoDerivs CC BY-NC-ND 4.0 ; DOAJ ; OpenAccess ; BIOSIS Previews ; IF >= 5 ; JCR ; NCBI Molecular Biology Database ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection ; Zoological Record
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 Record created 2015-02-03, last modified 2025-07-30


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