Title | Crystallization of the HigBA2 toxin-antitoxin complex from Vibrio cholerae. |
Publication Type | Journal Article |
Year of Publication | 2013 |
Authors | Hadži, S., A. Garcia-Pino, S. Martinez-Rodriguez, K. Verschueren, M. Christensen-Dalsgaard, K. Gerdes, J. Lah, and R. Loris |
Journal | Acta Crystallogr Sect F Struct Biol Cryst Commun |
Volume | 69 |
Issue | Pt 9 |
Pagination | 1052-9 |
Date Published | 2013 Sep |
Type of Article | ta |
ISSN | 1744-3091 |
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 P2(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 P3(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 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. |
DOI | 10.1107/S1744309113021490 |
Alternate Journal | Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. |
PubMed ID | 23989162 |
PubMed Central ID | PMC3758162 |
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