Open AccessOutrunning free radicals in room‐temperature macromolecular crystallography
Author(s) -
Owen Robin L.,
Axford Danny,
Nettleship Joanne E.,
Owens Raymond J.,
Robinson James I.,
Morgan Ann W.,
Doré Andrew S.,
Lebon Guillaume,
Tate Christopher G.,
Fry Elizabeth E.,
Ren Jingshan,
Stuart David I.,
Evans Gwyndaf
Publication year - 2012
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444912012553
Subject(s) - radical , macromolecule , synchrotron , crystallography , protein crystallization , chemistry , amorphous solid , crystal (programming language) , x ray crystallography , diffraction , materials science , crystallization , optics , physics , organic chemistry , biochemistry , programming language , computer science
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 γ Fc receptor IIIa), a virus (bovine enterovirus serotype 2) and a membrane protein (human A 2A 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.