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Updated: Jul 10, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
Published on: October 2, 2017
Expression, purification and preliminary X-ray diffraction studies of RebC
Laura M van Staalduinen1, Anupam Bhattacharya, Katherine Groom
1Department of Biochemistry, Queen's University, Kingston K7L 3N6, Canada.
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 .

