Cloning expression crystallization and preliminary X-ray characterization of cytochrome c 552 from a moderate thermophilic bacterium Hydrogenophilus thermoluteolus

摘要

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 aeruginosa (PA c 551). The PH c 552 gene was overexpressed as a correctly processed holoprotein in the Escherichia coli periplasm. The overexpressed PH c 552 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.