1University of South Bohemia in Ceske Budejovice, Faculty of Science, Branisovska 1760, 370 05 Ceske Budejovice
2Academy of Sciences of the Czech Republic, Center for Nanobiology and Structural Biology IMB, Zamek 136, 373 33 Nove Hrady
3iXpressGenes Inc.,601 Genome Way, Huntsville, AL 35810, USA
Crystallization of macromolecules and structural studies have an important role in a number of biological branches, such as molecular biology, pharmacology, enzymology or biochemistry. The main goal of this research was to optimalize crystallization conditions and obtain suitable monocrystals of a newly prepared and yet uncharacterized protein DH Tt80 from Thermococcus kodakarensis KOD1, which is considered to be sugar-phosphatase. The crystallization experiment was performed using the sitting drop vapour diffusion technique and crystallization kit SaltRx (Hampton Research, USA). Diffraction data were collected to the resolution about 2.0Å and will be used for further research, mainly for solving the structure of sugar-phosphatase DH Tt80.
Acknowledgement: The work was supported from ERDF Project No. CZ.02.1.01/0.0/0.0/15_003/0000441 and GACR 17-24321S.