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Serial femtosecond X‐ray diffraction of 30S ribosomal subunit microcrystals in liquid suspension at ambient temperature using an X‐ray free‐electron laser

Serial femtosecond X‐ray diffraction of 30S ribosomal subunit microcrystals in liquid suspension... High‐resolution ribosome structures determined by X‐ray crystallography have provided important insights into the mechanism of translation. Such studies have thus far relied on large ribosome crystals kept at cryogenic temperatures to reduce radiation damage. Here, the application of serial femtosecond X‐ray crystallography (SFX) using an X‐ray free‐electron laser (XFEL) to obtain diffraction data from ribosome microcrystals in liquid suspension at ambient temperature is described. 30S ribosomal subunit microcrystals diffracted to beyond 6 Å resolution, demonstrating the feasibility of using SFX for ribosome structural studies. The ability to collect diffraction data at near‐physiological temperatures promises to provide fundamental insights into the structural dynamics of the ribosome and its functional complexes. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Serial femtosecond X‐ray diffraction of 30S ribosomal subunit microcrystals in liquid suspension at ambient temperature using an X‐ray free‐electron laser

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References (68)

Publisher
Wiley
Copyright
© Demirci et al. 2013
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S174430911302099X
pmid
23989164
Publisher site
See Article on Publisher Site

Abstract

High‐resolution ribosome structures determined by X‐ray crystallography have provided important insights into the mechanism of translation. Such studies have thus far relied on large ribosome crystals kept at cryogenic temperatures to reduce radiation damage. Here, the application of serial femtosecond X‐ray crystallography (SFX) using an X‐ray free‐electron laser (XFEL) to obtain diffraction data from ribosome microcrystals in liquid suspension at ambient temperature is described. 30S ribosomal subunit microcrystals diffracted to beyond 6 Å resolution, demonstrating the feasibility of using SFX for ribosome structural studies. The ability to collect diffraction data at near‐physiological temperatures promises to provide fundamental insights into the structural dynamics of the ribosome and its functional complexes.

Journal

Acta Crystallographica Section FWiley

Published: Sep 1, 2013

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