Open AccessCrystallization and preliminary X‐ray analysis of 1 H ‐3‐hydroxy‐4‐oxoquinaldine 2,4‐dioxygenase from Arthrobacter nitroguajacolicus Rü61a: a cofactor‐devoid dioxygenase of the α/β‐hydrolase‐fold superfamily
Author(s) -
Steiner Roberto A.,
FrerichsDeeken Ursula,
Fetzner Susanne
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910701353x
Subject(s) - dioxygenase , cofactor , chemistry , crystallization , crystallography , arthrobacter , enzyme , tetragonal crystal system , stereochemistry , biochemistry , crystal structure , organic chemistry
1 H ‐3‐Hydroxy‐4‐oxoquinaldine 2,4‐dioxygenase (HOD) is a cofactor‐devoid dioxygenase that is involved in the anthranilate pathway of quinaldine degradation. HOD has been proposed to belong to the α/β‐hydrolase‐fold superfamily of enzymes. N‐terminally His 6 ‐tagged HOD has been crystallized by the hanging‐drop vapour‐diffusion method using sodium/potassium tartrate as a precipitant and CuCl 2 as an additive. The structure was solved by the single anomalous dispersion (SAD) technique using data collected to 3.5 Å resolution at the Cu absorption peak wavelength. The crystals belong to the primitive tetragonal space group P 4 3 2 1 2, with unit‐cell parameters a = b = 153.788, c = 120.872 Å.