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RABDAM: Quantifying specific radiation damage in individual protein crystal structures

Abstract:

Radiation damage remains one of the major limitations to accurate structure determination in protein crystallography (PX). Despite the use of cryo-cooling techniques, it is highly probable that a number of the structures deposited in the Protein Data Bank (PDB) have suffered substantial radiation damage as a result of the high flux densities of third generation synchrotron X-ray sources. Whereas the effects of global damage upon diffraction pattern reflection intensities are readily detectabl...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1107/S1600576718002509

Authors


Shelley, KL More by this author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
ORCID:
0000-0003-3825-6346
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
Oxford college:
Brasenose College
ORCID:
0000-0001-8329-5665
Moritz– Heyman Scholarship Programme More from this funder
Publisher:
International Union of Crystallography Publisher's website
Journal:
Journal of Applied Crystallography Journal website
Volume:
51
Issue:
Pt 2
Pages:
552-559
Publication date:
2018-03-28
Acceptance date:
2018-02-12
DOI:
EISSN:
1600-5767
ISSN:
0021-8898
Pubs id:
pubs:843555
URN:
uri:6a1a8df5-1538-42b4-964c-1aba6dac8fde
UUID:
uuid:6a1a8df5-1538-42b4-964c-1aba6dac8fde
Local pid:
pubs:843555

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