Crystallization of the HigBA2 toxin-antitoxin complex from Vibrio cholerae.

ABSTRACT: The genome of Vibrio cholerae encodes two higBA toxin-antitoxin (TA) modules that are activated by amino-acid starvation. Here, the TA complex of the second module, higBA2, as well as the C-terminal domain of the corresponding HigA2 antitoxin, have been purified and crystallized. The HigBA2 complex crystallized in two crystal forms. Crystals of form I belonged to space group P2(1)2(1)2, with unit-cell parameters a = 129.0, b = 119.8, c = 33.4?Å, and diffracted to 3.0?Å resolution. The asymmetric unit is likely to contain a single complex consisting of two toxin monomers and one antitoxin dimer. The second crystal form crystallized in space group P3(2)21, with unit-cell parameters a = 134.5, c = 55.4?Å. These crystals diffracted to 2.2?Å resolution and probably contain a complex with a different stoichiometry. Crystals of the C-terminal domain of HigA2 belonged to space group C2, with unit-cell parameters a = 115.4, b = 61.2, c = 73.8?Å, ? = 106.7°, and diffracted to 1.8?Å resolution.

SUBMITTER: Hadzi S 

PROVIDER: S-EPMC3758162 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature