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Crystallization and preliminary X-ray diffraction studies of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123

An NAD(+)-dependent psychrophilic alcohol dehydrogenase (ADH) from the Antarctic psychrophile Moraxella sp. TAE123 has been purified to homogeneity. The enzyme consists of four identical subunits, each containing two Zn ions. Protein crystals suitable for X-ray diffraction were obtained under optimi...

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Autores principales: Papanikolau, Yannis, Tsigos, Iason, Papadovasilaki, Maria, Bouriotis, Vassilis, Petratos, Kyriacos
Formato: Artigo
Lenguaje:Inglês
Publicado: International Union of Crystallography 2005
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC1952263/
https://ncbi.nlm.nih.gov/pubmed/16511007
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309105002253
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