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A departure from a linear or an exponential intensity decay in the diffracting power of protein crystals as a function of absorbed dose is reported. The observation of a lag phase raises the possibility of collecting significantly more data from crystals held at room temperature before an intolerable intensity decay is reached. A simple model accounting for the form of the intensity decay is reintroduced and is applied for the first time to high frame-rate room-temperature data collection.

Original publication

DOI

10.1107/S1399004714005379

Type

Journal article

Journal

Acta Crystallogr D Biol Crystallogr

Publication Date

05/2014

Volume

70

Pages

1248 - 1256

Keywords

dose rate, macromolecular crystallography, radiation damage, room temperature, Crystallography, X-Ray, Enterovirus, Bovine, Foot-and-Mouth Disease Virus, Models, Theoretical, Proteins, Temperature