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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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Auteurs principaux: Papanikolau, Yannis, Tsigos, Iason, Papadovasilaki, Maria, Bouriotis, Vassilis, Petratos, Kyriacos
Format: Artigo
Langue:Inglês
Publié: International Union of Crystallography 2005
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Accès en ligne: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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