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Purification and Crystallization of a Lysr-Type Transcriptional Regulator Cbnr from Ralstonia Eutropha Nh9

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Abstract:



CbnR, a LysR-type transcriptional regulator from Ralstonia eutropha NH9, has been crystallized by the vapor-diffusion method. It is intriguing to note that the different mixing ratios between the protein and reservoir solutions resulted in the different crystal forms. These crystals have the symmetry of the orthorhombic system with space groups P21212 and P2 1 2 1 2 1.





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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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