ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Crystallographic analysis of new psychrophilic haloalkane dehalogenases: DpcA from Psychrobacter cryohalolentis K5 and DmxA from Marinobacter sp. ELB17.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Psychrophilic enzymes: structural adaptation, pharmaceutical and industrial applications.Applied microbiology and biotechnology · 2021Review
- Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic BacteriumMicroorganisms · 2019Article
- Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Dehalogenases: From Improved Performance to Potential Microbial Dehalogenation Applications.Molecules (Basel, Switzerland) · 2018Review
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9 authors.
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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.
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