1 Section II. Building 18.2, Department of Cellular and Molecular Medicine, Faculty of Health and Medical Sciences, Københavns Universitet2 unknown3 Functional Genomics, Department of Biology, Faculty of Science, Københavns Universitet4 Section II. Building 18.2, Department of Cellular and Molecular Medicine, Faculty of Health and Medical Sciences, Københavns Universitet5 Functional Genomics, Department of Biology, Faculty of Science, Københavns Universitet
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 P21212, 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 P3221, 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, β = 106.7°, and diffracted to 1.8 Å resolution.
Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 2013, Vol 69, Issue Pt 9, p. 1052-9