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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jun 1;61(Pt 6):577-80. doi: 10.1107/S1744309105014557. Epub 2005 Jun 1.

Abstract

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%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Cloning, Molecular
  • Crystallization / methods
  • Dioxygenases / chemistry*
  • Electron Transport
  • Escherichia coli / genetics
  • Ferredoxins / chemistry
  • Oxygenases / chemistry
  • X-Ray Diffraction

Substances

  • Bacterial Proteins
  • Ferredoxins
  • Oxygenases
  • Dioxygenases
  • carbazole 1,9a-dioxygenase