Crystallization of the HigBA2 toxin-antitoxin complex from Vibrio cholerae
Research output: Contribution to journal › Journal article › Research › peer-review
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.
Original language | English |
---|---|
Journal | Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online |
Volume | 69 |
Issue number | Pt 9 |
Pages (from-to) | 1052-9 |
Number of pages | 8 |
ISSN | 1744-3091 |
DOIs | |
Publication status | Published - Sep 2013 |
ID: 49868581