Similarities and differences in radiation damage at 100 K versus 160 K in a crystal of thermolysin
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...
| Veröffentlicht in: | Journal of synchrotron radiation. - 1994. - 18(2011), Pt 3 vom: 18. Mai, Seite 329-37 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
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2011
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| Zugriff auf das übergeordnete Werk: | Journal of synchrotron radiation |
| Schlagworte: | Journal Article |
| Zusammenfassung: | 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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| Beschreibung: | Date Completed 16.08.2011 Date Revised 28.04.2011 published: Print-Electronic Citation Status PubMed-not-MEDLINE |
| ISSN: | 1600-5775 |
| DOI: | 10.1107/S0909049511007631 |