Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase component of carbazole 1,9a-dioxygenase from Novosphingobium sp. KA1.
Carbazole 1,9a-dioxygenase (CARDO) is the initial enzyme of the carbazole-degradation pathway. The CARDO of Novosphingobium sp. KA1 consists of a terminal oxygenase, a putidaredoxin-type ferredoxin and a ferredoxin-NADH oxidoreductase (Red) and is classified as a class IIA Rieske oxygenase. Red from KA1 was crystallized at 278 K by the hanging-drop vapour-diffusion method using PEG 4000. The crystal diffracted to 1.58 A resolution and belonged to space group P3(2), with unit-cell parameters a = b = 92.2, c = 78.6 A, alpha = gamma = 90, beta = 120 degrees . Preliminary analysis of the X-ray diffraction data revealed that the asymmetric unit contained two Red monomers. The crystal appeared to be a merohedral twin, with a twin fraction of 0.32 and twin law (-h, -k, l).
Umeda
Takashi
T
Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
Katsuki
Junichi
J
Ashikawa
Yuji
Y
Usami
Yusuke
Y
Inoue
Kengo
K
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*; D005287:Ferredoxin-NADP Reductase / Q000737:chemistry*; D042301:Sphingomonadaceae / Q000201:enzymology*
D001426:Bacterial Proteins; D049308:Dioxygenases; C108434:carbazole 1,9a-dioxygenase; D005287:Ferredoxin-NADP Reductase