Crystallization and preliminary crystallographic analysis of the ferredoxin 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 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 A resolution and belong to space group P4(1)2(1)2.
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 / Q000032:analysis / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D049308:Dioxygenases / Q000032:analysis / Q000737:chemistry*; D005288:Ferredoxins / Q000032:analysis / Q000737:chemistry*; D009618:Nocardiaceae / Q000201:enzymology*
D001426:Bacterial Proteins; D005288:Ferredoxins; D049308:Dioxygenases; C108434:carbazole 1,9a-dioxygenase