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 optimized salting-out crystallization conditions using ammonium sulfate as a precipitating agent. The crystals are hexagonal bipyramids and belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = 136.4, c = 210.7 A. They contain one protein homotetramer in the asymmetric unit. Diffraction data were collected to 2.2 A under cryogenic conditions using synchrotron radiation.
Papanikolau
Yannis
Y
Institute of Molecular Biology and Biotechnology-FORTH, PO Box 1527, 71110 Heraklion, Greece.
Tsigos
Iason
I
Papadovasilaki
Maria
M
Bouriotis
Vassilis
V
Petratos
Kyriacos
K
D000426:Alcohol Dehydrogenase / Q000737:chemistry* / Q000302:isolation & purification; D000864:Antarctic Regions; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification; D003460:Crystallization; D009016:Moraxella / Q000201:enzymology* / Q000302:isolation & purification; D012623:Seawater / Q000382:microbiology; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D000426:Alcohol Dehydrogenase