Expression, purification and preliminary X-ray diffraction studies of RebC
- Department of Biochemistry, Queen’s University, Kingston K7L 3N6 (Canada)
- Department of Chemistry, Queen’s University, Kingston K7L 3N6 (Canada)
The flavin-dependent monooxygenase RebC has been crystallized by the hanging-drop vapour-diffusion method and initial X-ray diffraction analysis has been completed. 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 Å; the crystals belonged to space group P2{sub 1}, with unit-cell parameters a = 63.08, b = 77.85, c = 63.94 Å, α = γ = 90, β = 108.11°.
- OSTI ID:
- 22360423
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 11 Vol. 63; ISSN ACSFCL; ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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