Crystallization and preliminary X-ray diffraction analysis of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26

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 Angstrom using synchrotron X-ray under cryogenic (100 K) conditions. They belong to the orthorhombic space group P2(1)2(1)2 with unit-cell parameters a = 50.29, b = 71.70, c = 72.73 Angstrom. The asymmetric unit contains one molecule of the enzyme.