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 optimize...

Full description

Saved in:
Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2005-02, Vol.61 (2), p.246-248
Main Authors: Papanikolau, Yannis, Tsigos, Iason, Papadovasilaki, Maria, Bouriotis, Vassilis, Petratos, Kyriacos
Format: Article
Language:English
Subjects:
Alcohol Dehydrogenase - chemistry
Alcohol Dehydrogenase - isolation & purification
alcohol dehydrogenases
Antarctic Regions
Bacterial Proteins - chemistry
Bacterial Proteins - isolation & purification
CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
Crystallization Communications
MOLECULAR STRUCTURE
Moraxella - enzymology
Moraxella - isolation & purification
Moraxella sp. TAE123
NAD(H)-dependent
psychrophilic
Seawater - microbiology
X-RAY DIFFRACTION
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 P3121 or P3221, 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.
ISSN:1744-3091
1744-3091
DOI:10.1107/S1744309105002253