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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...
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Päätekijät: | , , , , |
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Aineistotyyppi: | Artigo |
Kieli: | Inglês |
Julkaistu: |
International Union of Crystallography
2011
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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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