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Crystallization of the Effector-Binding Domain of Repressor DeoR from Bacillus subtilis
- 1.0392314 - ÚOCHB 2014 RIV US eng J - Journal Article
Písačková, Jana - Procházková, Kateřina - Fábry, Milan - Řezáčová, Pavlína
Crystallization of the Effector-Binding Domain of Repressor DeoR from Bacillus subtilis.
Crystal Growth & Design. Roč. 13, č. 2 (2013), s. 844-848. ISSN 1528-7483. E-ISSN 1528-7505
R&D Projects: GA MŠMT ME08016; GA MŠMT(CZ) LK11205; GA ČR GA203/09/0820
Institutional research plan: CEZ:AV0Z50520514; CEZ:AV0Z40550506
Keywords : X-ray crystallography * deoxyribonucleoside regulator * Bacillus subtilis * thermofluor assay
Subject RIV: CE - Biochemistry
Impact factor: 4.558, year: 2013
The DeoR repressor of Bacillus subtilis negatively regulates the expression of the enzymes needed for the metabolism of deoxyribonucleosides and deoxyribose. To gain structural information on the regulation of DeoR function by a small molecular ligand, we prepared crystals of the C-terminal domain of DeoR in its free form and in complex with the effector molecule deoxyribose-5-phosphate. To develop the optimal procedure for crystallization, we have employed the thermofluor assay as a tool for the optimization of protein crystallizability. The monocrystals of three crystal forms were used to collect complete sets of diffraction data at a synchrotron radiation source and will be used to determine the DeoR crystal structure.
Permanent Link: http://hdl.handle.net/11104/0221218
Number of the records: 1