Expression, Purification and Preliminary Diffraction Studies of CmlS

Journal Article · Thu Jan 01 00:00:00 EST 2009 · Acta Crystallographica Section F: Structural Biology and Crystallization Communications

DOI:https://doi.org/10.1107/S1744309108043091· OSTI ID:980206

Latimer, R; Podzelinska, K; Soares, A; Bhattacharya, A; Vining, L; Jia, Z; Zechel, D

CmlS, a flavin-dependent halogenase (FDH) present in the chloramphenicol-biosynthetic pathway in Streptomyces venezuelae, directs the dichlorination of an acetyl group. The reaction mechanism of CmlS is of considerable interest as it will help to explain how the FDH family can halogenate a wide range of substrates through a common mechanism. The protein has been recombinantly expressed in Escherichia coli and purified to homogeneity. The hanging-drop vapour-diffusion method was used to produce crystals that were suitable for X-ray diffraction. Data were collected to 2.0 Angstroms resolution. The crystal belonged to space group C2, with unit-cell parameters

• Research Organization: Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: DE-AC02-98CH10886
• OSTI ID: 980206
• Report Number(s): BNL-93124-2010-JA; TRN: US201015%%1591
• Journal Information: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 65
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
DIFFRACTION
ESCHERICHIA COLI
PROTEINS
PURIFICATION
REACTION KINETICS
RESOLUTION
SPACE GROUPS
STREPTOMYCES
SUBSTRATES
X-RAY DIFFRACTION
national synchrotron light source