Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 69, Part 9 (September 2013)


crystallization communications



Acta Cryst. (2013). F69, 1052-1059    [ doi:10.1107/S1744309113021490 ]

Crystallization of the HigBA2 toxin-antitoxin complex from Vibrio cholerae

S. Hadzi, A. Garcia-Pino, S. Martinez-Rodriguez, K. Verschueren, M. Christensen-Dalsgaard, K. Gerdes, J. Lah and R. Loris

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, [beta] = 106.7°, and diffracted to 1.8 Å resolution.

Keywords: toxin-antitoxin modules; ribonucleases; intrinsic disorder; macromolecular complexes; persistence.


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