Journal
CRYSTAL GROWTH & DESIGN
Volume 13, Issue 2, Pages 844-848Publisher
AMER CHEMICAL SOC
DOI: 10.1021/cg301551v
Keywords
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Funding
- Ministry of Education of the Czech Republic [ME08016, LK11205]
- Academy of Sciences of the Czech Republic [AV0Z40550506, AV0Z50520514]
- Grant Agency of the Czech Republic [GA203/09/0820]
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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.
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