Expression, purification and preliminary X-ray diffraction studies of RebC

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Nov 1;63(Pt 11):980-2. doi: 10.1107/S1744309107051640. Epub 2007 Oct 26.

Abstract

The flavin-dependent monooxygenase RebC is a key enzyme in the biosynthesis of the indolocarbazole rebeccamycin. The synthesis of rebeccamycin is of great interest as it has been shown to be a natural antitumour agent. The enzyme has been recombinantly expressed in Escherichia coli and purified to homogeneity. Hanging-drop vapour diffusion in combination with microseeding was used to obtain suitable crystals for X-ray diffraction. Data were collected to 2.4 A; the crystals belonged to space group P2(1), with unit-cell parameters a = 63.08, b = 77.85, c = 63.94 A, alpha = gamma = 90, beta = 108.11 degrees .

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actinomycetales / enzymology
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / metabolism
  • Mixed Function Oxygenases / biosynthesis*
  • Mixed Function Oxygenases / chemistry*
  • Mixed Function Oxygenases / isolation & purification

Substances

  • Mixed Function Oxygenases
  • RebC protein, Lechevalieria aerocolonigenes