Crystallization and preliminary X-ray analysis of a novel haloalkane dehalogenase DbeA from Bradyrhizobium elkani USDA94

0343421 - ÚOCHB 2011 RIV GB eng J - Journal Article
Prudnikova, T. - Mozga, T. - Řezáčová, Pavlína - Chaloupková, R. - Sato, Y. - Nagata, Y. - Brynda, Jiří - Kutý, Michal - Damborský, J. - Kutá-Smatanová, Ivana
Crystallization and preliminary X-ray analysis of a novel haloalkane dehalogenase DbeA from Bradyrhizobium elkani USDA94.
Acta Crystallographica Section F-Structural Biology and Crystallization Communications. F65, č. 4 (2009), s. 353-356. ISSN 1744-3091. E-ISSN 2053-230X
R&D Projects: GA MŠMT(CZ) LC06010
Institutional research plan: CEZ:AV0Z40550506; CEZ:AV0Z60870520; CEZ:AV0Z50520514
Keywords : protein crystallization * X-ray analysis * dehalogenase
Subject RIV: CC - Organic Chemistry
Impact factor: 0.551, year: 2009

A novel enzyme, DbeA, belonging to the haloalkane dehalogenase family (EC 3.8.1.5) was isolated from Bradyrhizobium elkani USDA94. In order to understand the unique activity and specificity of DbeA, its mutant variant DbeA1, which carries the unique fragment of DbjA, was also constructed. Both wild-type DbeA and DbeA1 were crystallized using the sitting-drop vapour-diffusion method. The crystals of DbeA belonged to the primitive orthorhombic space group P2(1)2(1)2(1), while the crystals of DbeA1 belonged to the monoclinic space group C2. Diffraction data were collected to 2.2 A resolution for both DbeA and DbeA1 crystals.
Permanent Link: http://hdl.handle.net/11104/0185903