The main goal is focused on crystalization study of newly prepared haloalkan dehalogenase DgaA from bacteria Glaciecola agarylitica NO2. The main target of this work is getting acquianted with methods of protein crystalization and usage of those methods for preparation of suitable DgaA protein crystals of that will be used for X-ray structural analysis. An essential requirement for using X-ray diffraction is to produce well ordered crystals without defects that are large enough to provide diffraction data after passing the X-ray beam. The crystallization experiment was performed using the sitting drop vapour diffusion techniques and crystallization screen Index HR2-144 (Hampton Research, USA). Results from difraction analysis of DgaA crystals will be starting point for further research focused on structure determination and and description of protein function.
Acknowledgement: The work was supported from GACR 17-24321S.