Crystallization and preliminary X-ray analysis of an enantioselective halohydrin dehalogenase from Agrobacterium radiobacter AD1.
Halohydrin dehalogenases are key enzymes in the bacterial degradation of vicinal halopropanols and structurally related nematocides. Crystals of the enantioselective halohydrin dehalogenase HheC from Agrobacterium radiobacter AD1 have been obtained at room temperature from hanging-drop vapour-diffusion experiments against 50-70% saturated ammonium sulfate solution at pH 6.5-7.3. The crystals belong to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 104.5, c = 121.4 A, and contain two monomers in the asymmetric unit. The crystals diffract to 3.0 A resolution with X-rays from a Cu Kalpha rotating-anode generator.
de Jong
René M
RM
Laboratory of Biophysical Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Rozeboom
Henriëtte J
HJ
Kalk
Kor H
KH
Tang
Lixia
L
Janssen
Dick B
DB
Dijkstra
Bauke W
BW
D003460:Crystallization; D018360:Crystallography, X-Ray; D006867:Hydrolases / Q000737:chemistry*; D011487:Protein Conformation; D012231:Rhizobium / Q000201:enzymology*; D013237:Stereoisomerism
D006867:Hydrolases; C430848:halohydrin dehalogenase