Crystallization and preliminary X-ray diffraction studies of the terminal oxygenase component of carbazole 1,9a-dioxygenase from Nocardioides aromaticivorans IC177.
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 A resolution and belong to space group C2.
Inoue
Kengo
K
Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
Ashikawa
Yuji
Y
Usami
Yusuke
Y
Noguchi
Haruko
H
Fujimoto
Zui
Z
Yamane
Hisakazu
H
Nojiri
Hideaki
H
D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D049308:Dioxygenases / Q000737:chemistry*; D009618:Nocardiaceae / Q000201:enzymology*
D001426:Bacterial Proteins; D049308:Dioxygenases; C108434:carbazole 1,9a-dioxygenase