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Outrunning free radicals in room-temperature macromolecular crystallography

DOI: 10.1107/S0907444912012553 DOI Help
PMID: 22751666 PMID Help

Authors: Robin Owen (Diamond Light Source) , Danny Axford (Diamond Light Source) , Joanne E. Nettleship (Research Complex at Harwell, Rutherford Appleton Laboratory, Division of Structural Biology, The Henry Wellcome Building for Genomic Medicine) , Raymond J. Owens (Harwell, Rutherford Appleton Laboratory, Research Complex at Harwell, Rutherford Appleton Laboratory, Division of Structural Biology, The Henry Wellcome Building for Genomic Medicine) , James I. Robinson (University of Leeds) , Ann W. Morgan (University of Leeds) , Andrew S. Dore (Heptares Therapeutics Ltd,) , Guillaume Lebon (MRC Laboratory of Molecular Biology) , Christopher G. Tate (MRC Laboratory of Molecular Biology Cambridge) , Elizabeth E. Fry (Division of Structural Biology, The Henry Wellcome Building for Genomic Medicine) , Jingshan Ren (Division of Structural Biology, The Henry Wellcome Building for Genomic Medicine) , Dave Stuart (Diamond Light Source) , Gwyndaf Evans (Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section D , VOL 68 (7) , PAGES 810-818

State: Published (Approved)
Published: July 2012

Open Access Open Access

Abstract: A significant increase in the lifetime of room-temperature macromolecular crystals is reported through the use of a high-brilliance X-ray beam, reduced exposure times and a fast-readout detector. This is attributed to the ability to collect diffraction data before hydroxyl radicals can propagate through the crystal, fatally disrupting the lattice. Hydroxyl radicals are shown to be trapped in amorphous solutions at 100 K. The trend in crystal lifetime was observed in crystals of a soluble protein (immunoglobulin [gamma] Fc receptor IIIa), a virus (bovine enterovirus serotype 2) and a membrane protein (human A2A adenosine G-protein coupled receptor). The observation of a similar effect in all three systems provides clear evidence for a common optimal strategy for room-temperature data collection and will inform the design of future synchrotron beamlines and detectors for macro­molecular crystallography.

Journal Keywords: Radiation Damage; Room Temperature; Dose Rate; Free Radicals

Subject Areas: Biology and Bio-materials


Instruments: I24-Microfocus Macromolecular Crystallography

Added On: 06/09/2012 16:57

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