Protein crystallography is a field of study of the three-dimensional structure of biological macromolecules. Based on the knowledge of the atomic structure of the studied biomacromolecules, it is possible to describe the processes in the cell or the catalytic reaction. An important biophysical method for determining the structure of biological macromolecules is X-ray diffraction. 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 main goal of this research was to obtain suitable monocrystals of newly prepared protein Tt81 from Thermococcus thioreducens, which is considered to be haloacid dehalogenase. The crystallization experiment was performed using the microbatch and the sitting drop vapour diffusion techniques and crystallization screen Index HR2-144 (Hampton Research, USA). Diffraction data were collected to the resolution about 2.5 Å and will be used for further research, mainly for solving the structure of protein Tt81.
Acknowledgement: The work was supported from ERDF Project No. CZ.02.1.01/0.0/0.0/15_003/0000441 and GACR 17-24321S.