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Crystallization and preliminary X-ray analysis of a novel haloalkane dehalogenase DbeA from Bradyrhizobium elkani USDA94
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SYSNO ASEP 0343421 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Crystallization and preliminary X-ray analysis of a novel haloalkane dehalogenase DbeA from Bradyrhizobium elkani USDA94 Author(s) Prudnikova, T. (CZ)
Mozga, T. (CZ)
Řezáčová, Pavlína (UOCHB-X) RID, ORCID
Chaloupková, R. (CZ)
Sato, Y. (JP)
Nagata, Y. (JP)
Brynda, Jiří (UMG-J) RID
Kutý, Michal (UEK-B)
Damborský, J. (CZ)
Kutá-Smatanová, Ivana (UEK-B) RIDNumber of authors 10 Source Title Acta Crystallographica Section F-Structural Biology and Crystallization Communications. - : Wiley - ISSN 1744-3091
F65, č. 4 (2009), s. 353-356Number of pages 4 s. Language eng - English Country GB - United Kingdom Keywords protein crystallization ; X-ray analysis ; dehalogenase Subject RIV CC - Organic Chemistry R&D Projects LC06010 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z40550506 - UOCHB-X (2005-2011) AV0Z60870520 - UEK-B (2005-2011) AV0Z50520514 - UMG-J (2005-2011) UT WOS 000264770000009 DOI 10.1107/S1744309109007039 Annotation 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. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Year of Publishing 2011
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