Purification and crystallization of a LysR-type transcriptional regulator CBNR from Ralstonia eutropha NH9.

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 P2(1)1(i)2 and P2(1)2(1)2(1).

Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: unusual combination of two subunit forms and molecular bases for causing and changing DNA bend.

The LysR-type transcriptional regulator (LTTR) proteins are one of the most common transcriptional regulators in prokaryotes. Here we report the crystal structure of CbnR, which is one of the LTTRs derived from Ralstonia eutropha NH9. This is the first crystal structure of a full-length LTTR.