Crystallization and preliminary X-ray diffraction studies of the putative haloalkane dehalogenase DppA fromPlesiocystis pacificaSIR-I
Copyright policy ) Xenia, Bogdanović; Martin, Hesseler; Gottfried J, Palm; Uwe T, Bornscheuer; Winfried, Hinrichs;
Crystallization and preliminary X-ray diffraction studies of the putative haloalkane dehalogenase DppA fromPlesiocystis pacificaSIR-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.
- University of Greifswald Germany
Hydrolases, Myxococcales, Crystallization, Crystallography, X-Ray
Hydrolases, Myxococcales, Crystallization, Crystallography, X-Ray
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This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
Citations provided by BIP!popularityPopularity provided by BIP!
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
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