Crystallization of the Effector-Binding Domain of Repressor DeoR from Bacillus subtilis

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• 作者：Jana P铆sa膷kov谩 ; Kate艡ina Proch谩zkov谩 ; Milan F谩bry ; Pavl铆na 艠ez谩膷ov谩
• 刊名：Crystal Growth & Design
• 出版年：2013
• 出版时间：February 6, 2013
• 年：2013
• 卷：13
• 期：2
• 页码：844-848
• 全文大小：294K
• 年卷期：v.13,no.2(February 6, 2013)
• ISSN：1528-7505

文摘

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.