Crystallographic analysis of new psychrophilic haloalkane dehalogenases: DpcA from Psychrobacter cryohalolentis K5 and DmxA from Marinobacter sp. ELB17

Katsiaryna Tratsiak, Oksana Degtjarik, Ivana Drienovska, Lukas Chrast, Pavlina Rezacova, Michal Kuty, Radka Chaloupkova, Jiri Damborsky, Ivana Kuta Smatanova*

*Corresponding author for this work

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

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 Å.

Original languageEnglish
Pages (from-to)683-688
Number of pages6
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume69
Issue number6
DOIs
Publication statusPublished - 1 Jan 2013
Externally publishedYes

Keywords

  • DmxA
  • DpcA
  • haloalkane dehalogenases
  • Marinobacter sp. ELB17
  • Psychrobacter cryohalolentis K5

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