title: Expression, purification and preliminary diffraction studies of CmlS.
abstract: 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 A resolution. The crystal belonged to space group C2, with unit-cell parameters a = 208.1, b = 57.7, c = 59.9 A, beta = 97.5 degrees .
authors.affiliation: Department of Chemistry, Queen's University, Kingston, Ontario, Canada.
authors.forename: Ryan
authors.initials: R
authors.lastname: Latimer
authors.forename: Kateryna
authors.initials: K
authors.lastname: Podzelinska
authors.forename: Alexei
authors.initials: A
authors.lastname: Soares
authors.forename: Anupam
authors.initials: A
authors.lastname: Bhattacharya
authors.forename: Leo C
authors.initials: LC
authors.lastname: Vining
authors.forename: Zongchao
authors.initials: Z
authors.lastname: Jia
authors.forename: David L
authors.initials: DL
authors.lastname: Zechel
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D012645:Selenomethionine; D016415:Sequence Alignment; D013302:Streptomyces / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D012645:Selenomethionine