Open AccessCrystallization and preliminary crystallographic analysis of the ferredoxin 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 - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107041437
Subject(s) - ferredoxin , carbazole , dioxygenase , crystallography , stereochemistry , chemistry , materials science , 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 ferredoxin component of carbazole 1,9a‐dioxygenase from Nocardioides aromaticivorans IC177 was crystallized at 293 K using the hanging‐drop vapour‐diffusion method with ammonium sulfate as the precipitant. The crystals, which were improved by macroseeding, diffract to 2.0 Å resolution and belong to space group P 4 1 2 1 2.