Open AccessCrystallization and preliminary X‐ray diffraction studies of the terminal oxygenase component of carbazole 1,9a‐dioxygenase from Nocardioides aromaticivorans IC177
Author(s) -
Inoue Kengo,
Ashikawa Yuji,
Usami Yusuke,
Noguchi Haruko,
Fujimoto Zui,
Yamane Hisakazu,
Nojiri Hideaki
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106044939
Subject(s) - carbazole , dioxygenase , ferredoxin , crystallography , stereochemistry , materials science , chemistry , photochemistry , organic chemistry , enzyme
Carbazole 1,9a‐dioxygenase (CARDO) catalyzes the dihydroxylation of carbazole by angular‐position (C9a) carbon bonding to the imino nitrogen and its adjacent C1 carbon. CARDO consists of a terminal oxygenase component and two electron‐transfer components: ferredoxin and ferredoxin reductase. The terminal oxygenase component (43.9 kDa) of carbazole 1,9a‐dioxygenase from Nocardioides aromaticivorans IC177 was crystallized at 293 K using the hanging‐drop vapour‐diffusion method with PEG 8000 as the precipitant. The crystals diffract to 2.3 Å resolution and belong to space group C 2.