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Spatial distribution of radiation damage to crystalline proteins at 25-300 K

Cornell Affiliated Author(s)

Author

M. Warkentin
R. Badeau
J.B. Hopkins
R.E. Thorne

Abstract

The spatial distribution of radiation damage (assayed by increases in atomic B factors) to thaumatin and urease crystals at temperatures ranging from 25 to 300 K is reported. The nature of the damage changes dramatically at approximately 180 K. Above this temperature the role of solvent diffusion is apparent in thaumatin crystals, as solvent-exposed turns and loops are especially sensitive. In urease, a flap covering the active site is the most sensitive part of the molecule and nearby loops show enhanced sensitivity. Below 180 K sensitivity is correlated with poor local packing, especially in thaumatin. At all temperatures, the component of the damage that is spatially uniform within the unit cell accounts for more than half of the total increase in the atomic B factors and correlates with changes in mosaicity. This component may arise from lattice-level, rather than local, disorder. The effects of primary structure on radiation sensitivity are small compared with those of tertiary structure, local packing, solvent accessibility and crystal contacts. © 2012 International Union of Crystallography Printed in Singapore - all rights reserved.

Date Published

Journal

Acta Crystallographica Section D: Biological Crystallography

Volume

68

Issue

9

Number of Pages

1108-1117,

URL

https://www.scopus.com/inward/record.uri?eid=2-s2.0-84865767993&doi=10.1107%2fS0907444912021361&partnerID=40&md5=e3c50172ed2c7765b181003bf3fa1a57

DOI

10.1107/S0907444912021361

Research Area

Group (Lab)

Robert Thorne Group

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