Crystallization and preliminary X-ray diffraction studies of the ferredoxin reductase component in the Rieske nonhaem iron oxygenase system carbazole 1,9a-dioxygenase

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt 6):499-502. doi: 10.1107/S174430910702163X. Epub 2007 May 12.

Abstract

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 A and belonged to space group P4(2)2(1)2, with unit-cell parameters a = b = 158.7, c = 81.4 A. The type II crystal was obtained in drops from which type I crystals had been removed; it diffracted to 2.60 A resolution and belonged to the same space group, with unit-cell parameters a = b = 161.8, c = 79.5 A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Crystallization
  • Dioxygenases / chemistry*
  • Electron Transport Complex III / chemistry*
  • Ferredoxin-NADP Reductase / chemistry*
  • Iron-Sulfur Proteins / chemistry*
  • Nonheme Iron Proteins / chemistry
  • X-Ray Diffraction

Substances

  • Bacterial Proteins
  • Iron-Sulfur Proteins
  • Nonheme Iron Proteins
  • Rieske iron-sulfur protein
  • Dioxygenases
  • carbazole 1,9a-dioxygenase
  • Ferredoxin-NADP Reductase
  • Electron Transport Complex III