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Cloning, expression, crystallization and preliminary X-ray characterization of cytochrome c (552) from a moderate thermophilic bacterium, Hydrogenophilus thermoluteolus
The amino-acid sequence of cytochrome c (552) (PH c (552)) from a moderately thermophilic bacterium, Hydrogenophilus thermoluteolus, was more than 50% identical to that of cytochrome c from an extreme thermophile, Hydrogenobacter thermophilus (HT c (552)), and from a mesophile, Pseudomonas aeruginos...
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| Hauptverfasser: | , , , , , , , , |
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| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
International Union of Crystallography
2005
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1952422/ https://ncbi.nlm.nih.gov/pubmed/16511051 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309105007761 |
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