Haloalkane dehalogenases (HLDs) are microbial enzymes that have attracted significant interest because of their ability to catalyze the irreversible hydrolysis of a wide range of halogenated compounds. These enzymes can be used as potential applicants in industrial catalysis, in the bioremediation and the biosensing of environmental pollutants. Novel haloalkane dehalogenase DgaA (EC 3.8.1.5, HLDs) belonging to the superfamily of α/β hydrolases, was isolated from a psychrophilic and moderately halophilic organism, Glaciecola agarilytica NO2, that was found in marine sediment collected from the East Sea, Korea. The purified protein dialyzed against 50mM Tris HCl buffer (pH 7.5) overnight and stored at 193 K was used for crystallization experiments in the concentration of 13.6 mg ml-1. Screening for crystallization conditions has been performed by Oryx crystallization robot (Douglas Instruments, Ltd., UK) using sitting drop vapour diffusion method. Commercial crystallization screen Index HR2-144 (Hampton Research, USA) was used for screening of DgaA crystallization conditions. Futher optimization to find successful crystallization conditions will be starting point for further research focused on structure determination and and description of protein function.
The work was supported from GACR 17-24321S.