Conformational variation of proteins at room temperature is not dominated by radiation damage
Protein crystallography data collection at synchrotrons is routinely carried out at cryogenic temperatures to mitigate radiation damage. Although damage still takes place at 100 K and below, the immobilization of free radicals increases the lifetime of the crystals by approximately 100-fold. Recent...
Ausführliche Beschreibung
Bibliographische Detailangaben
| Veröffentlicht in: | Journal of synchrotron radiation. - 1994. - 24(2017), Pt 1 vom: 01. Jan., Seite 73-82
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| 1. Verfasser: |
Russi, Silvia
(VerfasserIn) |
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| Weitere Verfasser: |
González, Ana,
Kenner, Lillian R,
Keedy, Daniel A,
Fraser, James S,
van den Bedem, Henry |
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| Format: | Online-Aufsatz
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| Sprache: | English |
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| Veröffentlicht: |
2017
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| Zugriff auf das übergeordnete Werk: | Journal of synchrotron radiation
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| Schlagworte: | Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
conformational dynamics
cryo-temperature
radiation damage
room temperature
Proteins |
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