Expression, purification, crystallization and preliminary crystallographic analysis of osmotically inducible protein C
Selenium‐incorporated osmotically inducible protein C from the thermophilic bacterium Thermus thermophilus was overexpressed, purified and crystallized. The crystals belong to space group P1, with unit‐cell parameters a = 37.58, b = 40.95, c = 48.14 Å, α = 76.93, β = 74.04, γ = 64.05°. Five data set...
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Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2004-02, Vol.60 (2), p.357-358 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Selenium‐incorporated osmotically inducible protein C from the thermophilic bacterium Thermus thermophilus was overexpressed, purified and crystallized. The crystals belong to space group P1, with unit‐cell parameters a = 37.58, b = 40.95, c = 48.14 Å, α = 76.93, β = 74.04, γ = 64.05°. Five data sets were collected from a single crystal to 1.6 Å using synchrotron radiation for MAD phasing. Self‐rotation functions and the Matthews coefficient are consistent with two molecules in the asymmetric unit. |
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ISSN: | 1399-0047 0907-4449 1399-0047 |
DOI: | 10.1107/S0907444903027458 |