Open AccessCrystallization and preliminary X‐ray diffraction studies of a terminal oxygenase of carbazole 1,9a‐dioxygenase from Novosphingobium sp. KA1
Author(s) -
Umeda Takashi,
Katsuki Junichi,
Ashikawa Yuji,
Usami Yusuke,
Inoue Kengo,
Noguchi Haruko,
Fujimoto Zui,
Yamane Hisakazu,
Nojiri Hideaki
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110034949
Subject(s) - dioxygenase , carbazole , monoclinic crystal system , ferredoxin , chemistry , crystallography , materials science , crystal structure , photochemistry , organic chemistry , enzyme
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 P 2 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.