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

San Hadzi, Abel Garcia Pino, Sergio Martinez-Rodriguez, Koen Verschueren, Mikkel Christensen-Dalsgaard, Kenn Gerdes, Jurij Lah, Remy Loris

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


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 A ? , and diffracted to 3.0 A ? 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 A ? . These crystals diffracted to 2.2 A ? 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 A ? , = 106.7, and diffracted to 1.8 A ? resolution.
Original languageEnglish
Pages (from-to)1052-1059
Number of pages8
JournalActa Crystallogr F Struct Biol Commun
Publication statusPublished - 2013


  • Toxin-antitoxin module
  • Structural biology
  • Macromolecular Crystallography
  • Persister


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