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).
Muraoka
Shin
S
Department of BioEngineering, Nagaoka University of Technology, Niigata, Japan.
Okumura
Rumi
R
Uragami
Yoshitaka
Y
Nonaka
Takamasa
T
Ogawa
Naoto
N
Miyashita
Kiyotaka
K
Senda
Toshiya
T
D016960:Agrobacterium tumefaciens / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray; D020118:Cupriavidus necator / Q000737:chemistry*; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D014157:Transcription Factors / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism
D001426:Bacterial Proteins; D014157:Transcription Factors; C073470:LysR protein, Bacteria; D004247:DNA