Abstract

Article info 2018 6 (1)    006  (01)   pp.  23 ~ 27
Title Crystallization and preliminary X-ray diffraction analysis of a toxin-antitoxin MazEF complex from the extremophile Deinococcus radiodurans
Authors Immanuel Dhanasingh1, Eunsil Choi2, Jihwan Hwang2 and Sung Haeng Lee1*
Institutions 1Department of Cellular and Molecular Medicine, Chosun University School of Medicine, Gwangju 501-759, Korea, 2Department of Microbiology, Pusan National University, Busan 46241, Korea *Correspondence: sunglee@chosun.ac.kr
Abstract Toxin–antitoxin (TA) systems are ubiquitous among most of prokaryotes and govern the cell death or growth arrest in response to environmental cues. TA systems are associated with adaptation of pathogens to unfavorable environments, indicating their potential as a target for antibiotics. Here, we purified and crystallized the TA complex from the extremophile Deinococcus radiodurans. The TA complex (DrMazEF) was co-expressed and pulled using the N-terminal glutathione S-transferase-tagged DrMazF. The complex was crystallized in 100 mM citric acid pH 3.5 containing 25% PEG3350. The crystal diffracted X-ray to a 2.6 Å resolution and belonged to the space group P212121, with the unit cell parameters a = 46.01, b = 74.04, and c = 138.26 Å. The asymmetric unit of the crystal had six molecules in two heterotrimeric complexes with a calculated Mathew’s coefficient of 1.84 Å3 Da-1 and a solvent content of 33.18%.