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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Bibliografische gegevens
Hoofdauteurs: Ichiki, Shin-ichi, Nakamura, Shota, Ohkubo, Tadayasu, Kobayashi, Yuji, Hasegawa, Jun, Uchiyama, Susumu, Nishihara, Hirofumi, Mizuta, Keiko, Sambongi, Yoshihiro
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: International Union of Crystallography 2005
Onderwerpen:
Crystallization Communications
Online toegang: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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