title: Expression, purification and preliminary X-ray characterization of DL-2-haloacid dehalogenase from Methylobacterium sp. CPA1.
abstract: DL-2-Haloacid dehalogenase from Methylobacterium sp. CPA1 (DL-DEX Mb) is a unique enzyme that catalyzes the dehalogenation reaction without the formation of an ester intermediate. A recombinant form of DL-DEX Mb has been expressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The crystal belongs to the hexagonal space group P6(3), with unit-cell parameters a = b = 186.2, c = 114.4 A. The crystals are likely to contain between four and eight monomers in the asymmetric unit, with a V(M) value of 4.20-2.10 A3 Da(-1). A self-rotation function revealed peaks on the chi = 180 degrees section. X-ray data have been collected to 1.75 A resolution.
authors.affiliation: Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
authors.forename: Rie
authors.initials: R
authors.lastname: Omi
authors.forename: Keiji
authors.initials: K
authors.lastname: Jitsumori
authors.forename: Takahiro
authors.initials: T
authors.lastname: Yamauchi
authors.forename: Susumu
authors.initials: S
authors.lastname: Ichiyama
authors.forename: Tatsuo
authors.initials: T
authors.lastname: Kurihara
authors.forename: Nobuyoshi
authors.initials: N
authors.lastname: Esaki
authors.forename: Nobuo
authors.initials: N
authors.lastname: Kamiya
authors.forename: Ken
authors.initials: K
authors.lastname: Hirotsu
authors.forename: Ikuko
authors.initials: I
authors.lastname: Miyahara
mesh_terms: D018360:Crystallography, X-Ray / Q000379:methods; D015971:Gene Expression Regulation, Enzymologic; D006867:Hydrolases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D020580:Methylobacterium / Q000201:enzymology*
chemical_list: D006867:Hydrolases; C034507:2-haloacid dehalogenase