Open AccessCrystallization and preliminary X‐ray diffraction studies of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123
Author(s) -
Papanikolau Yannis,
Tsigos Iason,
Papadovasilaki Maria,
Bouriotis Vassilis,
Petratos Kyriacos
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105002253
Subject(s) - psychrophile , homotetramer , crystallization , crystallography , ammonium sulfate , protein crystallization , chemistry , alcohol dehydrogenase , alcohol , enzyme , biochemistry , chromatography , organic chemistry , protein subunit , gene
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 optimized salting‐out crystallization conditions using ammonium sulfate as a precipitating agent. The crystals are hexagonal bipyramids and belong to space group P 3 1 21 or P 3 2 21, with unit‐cell parameters a = 136.4, c = 210.7 Å. They contain one protein homotetramer in the asymmetric unit. Diffraction data were collected to 2.2 Å under cryogenic conditions using synchrotron radiation.