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

Journal Article · · Acta Crystallographica. Section F
 [1]; ; ;  [2];  [3];  [4];  [5];  [1];  [1]
  1. Graduate School of Biosphere Science, Hiroshima University, 1-4-4 Kagamiyama, Higashi-Hiroshima, Hiroshima 739-8528 (Japan)
  2. Graduate School of Pharmaceutical Sciences, Osaka University, Suita 565-0871 (Japan)
  3. Daiichi Pharmaceutical Co. Ltd, Edogawa-ku, Tokyo 134-8630 (Japan)
  4. Graduate School of Engineering, Osaka University, Suita 565-0871 (Japan)
  5. Ibaraki University, Chu-ou 3-21-1, Ami-machi, Inashiki-gun, Ibaraki 300-0393 (Japan)
Cytochrome c{sub 552} of a moderate thermophile, H. thermoluteolus, was overexpressed in E. coli and crystallized for X-ray diffraction study. The amino-acid sequence of cytochrome c{sub 552} (PH c{sub 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{sub 552}), and from a mesophile, Pseudomonas aeruginosa (PA c{sub 551}). The PH c{sub 552} gene was overexpressed as a correctly processed holoprotein in the Escherichia coli periplasm. The overexpressed PH c{sub 552} has been crystallized by vapour diffusion from polyethylene glycol 4000 pH 6.5. The crystals belong to space group C222{sub 1}, 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.
OSTI ID:
22356111
Journal Information:
Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 4 Vol. 61; ISSN ACSFCL; ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English

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