Crystallographic Analysis of New Psychrophilic Haloalkane Dehalogenases: DpcA from Psychrobacter cryohalolentis K5 and DmxA from Marinobacter sp. ELB17

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Authors	TRATSIAK K. DEGTJARIK O. DRIENOVSKA I. CHRÁST Lukáš REZACOVA P. KUTY M. CHALOUPKOVÁ Radka DAMBORSKÝ Jiří KUTA SMATANOVA I.
Year of publication	2013
Type	Article in Periodical
Magazine / Source	Acta Crystallographica
MU Faculty or unit	Faculty of Science
Citation
Doi	http://dx.doi.org/10.1107/S1744309113012979
Field	Biochemistry
Keywords	Haloalkane Dehalogenases
Description	Haloalkane dehalogenases are hydrolytic enzymes with a broad range of potential practical applications such as biodegradation, biosensing, biocatalysis and cellular imaging. Two newly isolated psychrophilic haloalkane dehalogenases exhibiting interesting catalytic properties, DpcA from Psychrobacter cryohalolentis K5 and DmxA from Marinobacter sp. ELB17, were purified and used for crystallization experiments. After the optimization of crystallization conditions, crystals of diffraction quality were obtained. Diffraction data sets were collected for native enzymes and complexes with selected ligands such as 1-bromohexane and 1,2-dichloroethane to resolutions ranging from 1.05 to 2.49 A.
Related projects:	Centrum pro výzkum toxických látek v prostředí Structure-functional Relationships of Haloalkane Dehalogenases