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231224s2011 xx |||||o 00| ||eng c |
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|a 10.1107/S0909049511007631
|2 doi
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|a DE-627
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|a eng
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|a Juers, Douglas H
|e verfasserin
|4 aut
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|a Similarities and differences in radiation damage at 100 K versus 160 K in a crystal of thermolysin
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|c 2011
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 16.08.2011
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|a Date Revised 28.04.2011
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|a published: Print-Electronic
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|a Citation Status PubMed-not-MEDLINE
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|a 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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|a Journal Article
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|a Weik, Martin
|e verfasserin
|4 aut
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|i Enthalten in
|t Journal of synchrotron radiation
|d 1994
|g 18(2011), Pt 3 vom: 18. Mai, Seite 329-37
|w (DE-627)NLM09824129X
|x 1600-5775
|7 nnns
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773 |
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|g volume:18
|g year:2011
|g number:Pt 3
|g day:18
|g month:05
|g pages:329-37
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|u http://dx.doi.org/10.1107/S0909049511007631
|3 Volltext
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|d 18
|j 2011
|e Pt 3
|b 18
|c 05
|h 329-37
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