Crystallization and preliminary X-ray diffraction studies of the putative haloalkane dehalogenase DppA from Plesiocystis pacifica SIR-I.
DppA from Plesiocystis pacifica SIR-I is a putative haloalkane dehalogenase (EC 3.8.1.5) and probably catalyzes the conversion of halogenated alkanes to the corresponding alcohols. The enzyme was expressed in Escherichia coli BL21 and purified to homogeneity by ammonium sulfate precipitation and reversed-phase and ion-exchange chromatography. The DppA protein was crystallized by the vapour-diffusion method and protein crystals suitable for data collection were obtained in the orthorhombic space group P2(1)2(1)2. The DppA crystal diffracted X-rays to 1.9 A resolution using an in-house X-ray generator.
Bogdanović
Xenia
X
Molecular Structural Biology, Institute for Biochemistry, University of Greifswald, Felix-Hausdorff-Strasse 4, D-17489 Greifswald, Germany. xenia.bogdanovic@uni-greifswald.de
Hesseler
Martin
M
Palm
Gottfried J
GJ
Bornscheuer
Uwe T
UT
Hinrichs
Winfried
W
D003460:Crystallization; D018360:Crystallography, X-Ray; D006867:Hydrolases / Q000737:chemistry*; D009231:Myxococcales / Q000201:enzymology*
D006867:Hydrolases; C046137:haloalkane dehalogenase