Expression, Purification and Preliminary X-ray Diffraction Studies of RebC

Journal Article · Sun Dec 31 23:00:00 EST 2006 · Acta Crystallographica Section F: Structural Biology and Crystallization Communications

DOI:https://doi.org/10.1107/S1744309107051640· OSTI ID:960090

van Staalduinen, L; Bhattacharya, A; Groom, K; Zechel, D; Jia, Z

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 Angstroms; the crystals belonged to space group P21, with unit-cell parameters a = 63.08, b = 77.85, c = 63.94 Angstroms, {alpha} = {gamma} = 90, {beta} = 108.11 .

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 960090
• Report Number(s): BNL--83076-2009-JA
• Journal Information: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Journal Name: Acta Crystallographica Section F: Structural Biology and Crystallization Communications Vol. 63
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS
BIOSYNTHESIS
DIFFUSION
ENZYMES
ESCHERICHIA COLI
PURIFICATION
SPACE GROUPS
SYNTHESIS
X-RAY DIFFRACTION
national synchrotron light source