Journal
JOURNAL OF SYNCHROTRON RADIATION
Volume 20, Issue -, Pages 7-13Publisher
WILEY-BLACKWELL
DOI: 10.1107/S0909049512048303
Keywords
protein crystallography; radiation damage; room temperature; dose rate; temperature dependence
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Funding
- NCRR NIH HHS [RR-01646, P41 RR001646] Funding Source: Medline
- NIGMS NIH HHS [R01 GM065981, GM065981] Funding Source: Medline
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A series of studies that provide a consistent and illuminating picture of global radiation damage to protein crystals, especially at temperatures above similar to 200 K, are described. The radiation sensitivity shows a transition near 200 K, above which it appears to be limited by solvent-coupled diffusive processes. Consistent with this interpretation, a component of global damage proceeds on timescales of several minutes at 180 K, decreasing to seconds near room temperature. As a result, data collection times of order 1 s allow up to half of global damage to be outrun at 260 K. Much larger damage reductions near room temperature should be feasible using larger dose rates delivered using microfocused beams, enabling a significant expansion of structural studies of proteins under more nearly native conditions.
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