Cloning, expression, crystallization and preliminary X-ray characterization of cytochrome c552 from a moderate thermophilic bacterium, Hydrogenophilus thermoluteolus.
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 C222(1), with unit-cell parameters a = 48.98, b = 57.99, c = 56.20 A. The crystals diffract X-rays to around 2.1 A resolution.
Ichiki
Shin-ichi
S
Graduate School of Biosphere Science, Hiroshima University, 1-4-4 Kagamiyama, Higashi-Hiroshima, Hiroshima 739-8528, Japan.
Nakamura
Shota
S
Ohkubo
Tadayasu
T
Kobayashi
Yuji
Y
Hasegawa
Jun
J
Uchiyama
Susumu
S
Nishihara
Hirofumi
H
Mizuta
Keiko
K
Sambongi
Yoshihiro
Y
D003001:Cloning, Molecular; D003460:Crystallization / Q000379:methods; D003574:Cytochrome c Group / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D004926:Escherichia coli / Q000235:genetics; D016133:Polymerase Chain Reaction; D011549:Pseudomonas / Q000737:chemistry; D014835:Volatilization; D014961:X-Ray Diffraction
D003574:Cytochrome c Group; C022302:cytochrome C-552