Source:http://linkedlifedata.com/resource/pubmed/id/21525640
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
Pt 3
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| pubmed:dateCreated |
2011-4-28
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| pubmed:abstractText |
The temperature-dependence of radiation damage in macromolecular X-ray crystallography is currently much debated. Most protein crystallographic studies are based on data collected at 100 K. Data collection at temperatures below 100 K has been proposed to reduce radiation damage and above 100 K to be useful for kinetic crystallography that is aimed at the generation and trapping of protein intermediate states. Here the global and specific synchrotron-radiation sensitivity of crystalline thermolysin at 100 and 160 K are compared. Both types of damage are higher at 160 K than at 100 K. At 160 K more residue types are affected (Lys, Asp, Gln, Pro, Thr, Met, Asn) than at 100 K (Met, Asp, Glu, Lys). The X-ray-induced relative atomic B-factor increase is shown to correlate with the proximity of the atom to the nearest solvent channel at 160 K. Two models may explain the observed correlation: either an increase in static disorder or an increased attack of hydroxyl radicals from the solvent area of the crystal.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
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| pubmed:month |
May
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| pubmed:issn |
1600-5775
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:volume |
18
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
329-37
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| pubmed:year |
2011
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| pubmed:articleTitle |
Similarities and differences in radiation damage at 100 K versus 160 K in a crystal of thermolysin.
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| pubmed:affiliation |
Department of Physics, Whitman College, Walla Walla, WA 99362, USA.
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| pubmed:publicationType |
Journal Article
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