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 structures of the reaction intermediate and its homologue of an extradiol-cleaving catecholic dioxygenase.

BphC derived from Pseudomonas sp. strain KKS102 is an extradiol-cleaving catecholic dioxygenase. This enzyme contains a non-heme iron atom and plays an important role in degrading biphenyl/polychlorinated biphenyls (PCBs) in the microbe.