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• W2023784821 abstract "The amino-acid sequence of cytochrome c552 (PH c552) from a moderately thermophilic bacterium, Hydrogenophilus thermoluteolus, was more than 50% identical to that of cytochrome c from an extreme thermophile, Hydrogenobacter thermophilus (HT c552), and from a mesophile, Pseudomonas aeruginosa (PA c551). The PH c552 gene was overexpressed as a correctly processed holoprotein in the Escherichia coli periplasm. The overexpressed PH c552 has been crystallized by vapour diffusion from polyethylene glycol 4000 pH 6.5. The crystals belong to space group C2221, with unit-cell parameters a = 48.98, b = 57.99, c = 56.20 Å. The crystals diffract X-rays to around 2.1 Å resolution." @default.
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• W2023784821 date "2005-03-24" @default.
• W2023784821 modified "2023-09-26" @default.
• W2023784821 title "Cloning, expression, crystallization and preliminary X-ray characterization of cytochrome<i>c</i>₅₅₂from a moderate thermophilic bacterium,<i>Hydrogenophilus thermoluteolus</i>" @default.
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• W2023784821 doi "https://doi.org/10.1107/s1744309105007761" @default.
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