Crystallization and preliminary X-ray diffraction analysis of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
10329794
DOI
10.1107/s090744499900459x
PII: JN0058
Knihovny.cz E-resources
- MeSH
- Hydrolases chemistry isolation & purification MeSH
- Protein Conformation MeSH
- Crystallization MeSH
- Crystallography, X-Ray MeSH
- Pseudomonas enzymology MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- haloalkane dehalogenase MeSH Browser
- Hydrolases MeSH
Haloalkane hydrolytic dehalogenase LinB from Sphingomonas paucimobilis UT26, an enzyme which releases chloride or bromide anion from n-halogenated alkanes and has a broad range of substrate specificity, was crystallized using the hanging-drop vapour-diffusion method at 278 K. The best crystals were obtained by microseeding with a precipitant containing 18-20%(w/v) PEG 6000, 0.2 M calcium acetate and 0.1 M Tris-HCl pH 8.9. The crystals diffract to at least 1.60 A using synchrotron X-ray under cryogenic (100 K) conditions. They belong to the orthorhombic space group P21212 with unit-cell parameters a = 50.29, b = 71.70, c = 72.73 A. The asymmetric unit contains one molecule of the enzyme.
References provided by Crossref.org
Differences in crystallization of two LinB variants from Sphingobium japonicum UT26
