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Crystallization and preliminary X-ray diffraction studies of a hyperthermophilic Rieske protein variant (SDX-triple) with an engineered rubredoxin-like mononuclear iron site

In place of the Rieske [2Fe–2S] cluster, an archetypal mononuclear iron site has rationally been designed into a hyperthermophilic archaeal Rieske [2Fe–2S] protein (sulredoxin) from Sulfolobus tokodaii by three residue replacements with reference to the Pyrococcus furiosus rubredoxin sequence. The r...

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Hlavní autoři: Iwasaki, Toshio, Kounosu, Asako, Ohmori, Daijiro, Kumasaka, Takashi
Médium: Artigo
Jazyk:Inglês
Vydáno: International Union of Crystallography 2006
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2225183/
https://ncbi.nlm.nih.gov/pubmed/17012793
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309106034476
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