Open AccessExpression, crystallization and preliminary X‐ray crystallographic analysis of alcohol dehydrogenase (ADH) from Kangiella koreensis
Author(s) -
Ngo HoPhuongThuy,
Hong SeungHye,
Hong MyoungKi,
Pham TanViet,
Oh DeokKun,
Kang LinWoo
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113022008
Subject(s) - crystallization , crystallography , x ray , alcohol dehydrogenase , chemistry , materials science , alcohol , biochemistry , physics , organic chemistry , optics
Alcohol dehydrogenases (ADHs) are a group of dehydrogenase enzymes that facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of NAD + to NADH. In bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD + . The adh gene from Kangiella koreensis was cloned and the protein (KkADH) was expressed, purified and crystallized. A KkADH crystal diffracted to 2.5 Å resolution and belonged to the monoclinic space group P 2 1 , with unit‐cell parameters a = 94.1, b = 80.9, c = 115.6 Å, β = 111.9°. Four monomers were present in the asymmetric unit, with a corresponding V M of 2.55 Å 3 Da −1 and a solvent content of 51.8%.