Expression, purification and preliminary X-ray characterization of DL-2-haloacid dehalogenase from Methylobacterium sp. CPA1.
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.
Omi
Rie
R
Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
Jitsumori
Keiji
K
Yamauchi
Takahiro
T
Ichiyama
Susumu
S
Kurihara
Tatsuo
T
Esaki
Nobuyoshi
N
Kamiya
Nobuo
N
Hirotsu
Ken
K
Miyahara
Ikuko
I
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*
D006867:Hydrolases; C034507:2-haloacid dehalogenase