Crystallization and preliminary X-ray diffraction studies of a terminal oxygenase of carbazole 1,9a-dioxygenase from Novosphingobium sp. KA1.
Carbazole 1,9a-dioxygenase (CARDO) is the initial dioxygenase in the carbazole-degradation pathway of Novosphingobium sp. KA1. The CARDO from KA1 consists of a terminal oxygenase (Oxy), a putidaredoxin-type ferredoxin and a ferredoxin reductase. The Oxy from Novosphingobium sp. KA1 was crystallized at 277 K using the hanging-drop vapour-diffusion method with ammonium sulfate as the precipitant. Diffraction data were collected to a resolution of 2.1 Å. The crystals belonged to the monoclinic space group P2(1). Self-rotation function analysis suggested that the asymmetric unit contained two Oxy trimers; the Matthews coefficient and solvent content were calculated to be 5.9 Å(3) Da(-1) and 79.1%, respectively.
Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
Takashi
T
Umeda
Junichi
J
Katsuki
Yuji
Y
Ashikawa
Yusuke
Y
Usami
Kengo
K
Inoue
Haruko
H
Noguchi
Zui
Z
Fujimoto
Hisakazu
H
Yamane
Hideaki
H
Nojiri
D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D049308:Dioxygenases / Q000737:chemistry*; D020578:Sphingomonas / Q000201:enzymology*
D001426:Bacterial Proteins; D049308:Dioxygenases; C108434:carbazole 1,9a-dioxygenase