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

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 .

SUBMITTER: van Staalduinen LM 

PROVIDER: S-EPMC2339749 | biostudies-literature | 2007 Nov

REPOSITORIES: biostudies-literature

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

van Staalduinen Laura M LM   Bhattacharya Anupam A   Groom Katherine K   Zechel David L DL   Jia Zongchao Z  

Acta crystallographica. Section F, Structural biology and crystallization communications 20071026 Pt 11

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 grou  ...[more]

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