Article info Vol. 6  No. 2   pp.  33 ~ 36
Title Expression, purification, crystallization, and X-ray diffraction studies on a PadR-like protein from Bacillus cereus
Authors Sun Cheol Park1†, Kang-Cheon Lee1† and Sung-il Yoon1,2*
Institutions 1Division of Biomedical Convergence, College of Biomedical Science, Kangwon National University, Chuncheon 24341, Republic of Korea, 2Institute of Bioscience and Biotechnology, Kangwon National University, Chuncheon 24341, Republic of Korea *Correspondence: sungil@kangwon.ac.kr † Equal contributions
Abstract Transcriptional regulators that belong to the PadR family play a critical role in the regulation of various biological processes, such as detoxification, catabolism, toxin production, and antibiotic resistance. The structural basis of effector and DNA recognition by PadR has recently been provided through our previous structural study. However, it is unclear whether the mechanism is universally used by other PadR family members. As a first step to reveal the transcription regulatory mechanism of Bacillus cereus PadR-like protein (bcPLP), we expressed the bcPLP protein in Escherichia coli cells and purified it to homogeneity by chromatographic methods. bcPLP was crystallized in PEG 3350 solutions. A bcPLP crystal diffracted X-ray to 1.95Å resolution. Our analysis of the X-ray diffraction data indicates that the crystal belongs to space group P21212 and has two bcPLP chains in the asymmetric unit.