Open AccessCrystallization and preliminary X‐ray diffraction studies of the ferredoxin reductase component in the Rieske nonhaem iron oxygenase system carbazole 1,9a‐dioxygenase
Author(s) -
Ashikawa Yuji,
Uchimura Hiromasa,
Fujimoto Zui,
Inoue Kengo,
Noguchi Haruko,
Yamane Hisakazu,
Nojiri Hideaki
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910702163x
Subject(s) - ferredoxin , carbazole , dioxygenase , crystallography , crystallization , crystal (programming language) , resolution (logic) , materials science , reductase , chemistry , photochemistry , enzyme , organic chemistry , artificial intelligence , computer science , programming language
Carbazole 1,9a‐dioxygenase (CARDO), which consists of an oxygenase component (CARDO‐O) and the electron‐transport components ferredoxin (CARDO‐F) and ferredoxin reductase (CARDO‐R), catalyzes dihydroxylation at the C1 and C9a positions of carbazole. CARDO‐R was crystallized at 277 K using the hanging‐drop vapour‐diffusion method with the precipitant PEG 8000. Two crystal types (types I and II) were obtained. The type I crystal diffracted to a maximum resolution of 2.80 Å and belonged to space group P 4 2 2 1 2, with unit‐cell parameters a = b = 158.7, c = 81.4 Å. The type II crystal was obtained in drops from which type I crystals had been removed; it diffracted to 2.60 Å resolution and belonged to the same space group, with unit‐cell parameters a = b = 161.8, c = 79.5 Å.