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

Acta Crystallogr Sect F Struct Biol Cryst Commun

Department of Biochemistry, Queen's University, Kingston K7L 3N6, Canada.

Published: November 2007

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 .

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2339749PMC
http://dx.doi.org/10.1107/S1744309107051640DOI Listing

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