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Structure of a multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum

The crystal structure of an extremely thermostable multicopper oxidase (McoP) from the hyperthermophilic archaeon Pyrobaculum aerophilum was determined at a resolution of 2.0 Å. The overall fold was comprised of three cupredoxin-like domains and the main-chain coordinates of the enzyme were similar...

Täydet tiedot

Tallennettuna:
Bibliografiset tiedot
Päätekijät: Sakuraba, Haruhiko, Koga, Kohtaroh, Yoneda, Kazunari, Kashima, Yasuhiro, Ohshima, Toshihisa
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: International Union of Crystallography 2011
Aiheet:
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC3144789/
https://ncbi.nlm.nih.gov/pubmed/21795787
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309111018173
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