Crystallization and preliminary X-ray diffraction analysis of the electron-transfer complex between the terminal oxygenase component and ferredoxin in the Rieske non-haem iron oxygenase system carbazole 1,9a-dioxygenase.
Carbazole 1,9a-dioxygenase, 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. The electron-transport complex between CARDO-O and CARDO-F crystallizes at 293 K using hanging-drop vapour diffusion with the precipitant PEG MME 2000 (type I crystals) or PEG 3350 (type II). Blossom-shaped crystals form from a pile of triangular plate-shaped crystals. The type I crystal diffracts to a maximum resolution of 1.90 A and belongs to space group P2(1), with unit-cell parameters a = 97.1, b = 89.8, c = 104.9 A, alpha = gamma = 90, beta = 103.8 degrees. Diffraction data for the type I crystal gave an overall Rmerge of 8.0% and a completeness of 100%. Its VM value is 2.63 A3 Da(-1), indicating a solvent content of 53.2%.
Ashikawa
Yuji
Y
Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Tokyo 113-8657, Japan.
Fujimoto
Zui
Z
Noguchi
Haruko
H
Habe
Hiroshi
H
Omori
Toshio
T
Yamane
Hisakazu
H
Nojiri
Hideaki
H
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization / Q000379:methods; D049308:Dioxygenases / Q000737:chemistry*; D004579:Electron Transport; D004926:Escherichia coli / Q000235:genetics; D005288:Ferredoxins / Q000737:chemistry; D010105:Oxygenases / Q000737:chemistry; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D005288:Ferredoxins; D010105:Oxygenases; D049308:Dioxygenases; C108434:carbazole 1,9a-dioxygenase