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- Publisher
- Wiley
- Copyright
- International Union of Crystallography, 2013
- ISSN
- 1744-3091
- eISSN
- 1744-3091
- DOI
- 10.1107/S1744309113021490
- pmid
- 23989162
- Publisher site
- See Article on Publisher Site
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 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.
Journal
Acta Crystallographica Section F – Wiley
Published: Sep 1, 2013