Open AccessExpression, purification and preliminary X‐ray diffraction studies of RebC
Author(s) -
Van Staalduinen Laura M.,
Bhattacharya Anupam,
Groom Katherine,
Zechel David L.,
Jia Zongchao
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107051640
Subject(s) - escherichia coli , enzyme , chemistry , x ray , monooxygenase , crystallography , stereochemistry , biochemistry , gene , cytochrome p450 , optics , physics
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 P 2 1 , with unit‐cell parameters a = 63.08, b = 77.85, c = 63.94 Å, α = γ = 90, β = 108.11°.