Open AccessCrystallization of the HigBA2 toxin–antitoxin complex from Vibrio cholerae
Author(s) -
Hadži San,
GarciaPino Abel,
MartinezRodriguez Sergio,
Verschueren Koen,
ChristensenDalsgaard Mikkel,
Gerdes Kenn,
Lah Jurij,
Loris Remy
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113021490
Subject(s) - antitoxin , vibrio cholerae , crystallization , toxin , crystallography , dimer , resolution (logic) , cholera toxin , chemistry , stereochemistry , biology , bacteria , microbiology and biotechnology , biochemistry , genetics , organic chemistry , artificial intelligence , computer science
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 P 2 1 2 1 2, 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 P 3 2 21, 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 C 2, with unit‐cell parameters a = 115.4, b = 61.2, c = 73.8 Å, β = 106.7°, and diffracted to 1.8 Å resolution.