Crystallization of the HigBA2 toxin-antitoxin complex from Vibrio cholerae

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

doi:10.1107/S1744309113021490

Crystallization of the HigBA2 toxin-antitoxin complex from Vibrio cholerae

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

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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, 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	https://doi.org/10.1107/S1744309113021490
Publication status	Published - Sept 2013

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Hadǽi, S., Garcia-Pino, A., Martinez-Rodriguez, S., Verschueren, K., Christensen-Dalsgaard, M., Gerdes, K., Lah, J., & Loris, R. (2013). Crystallization of the HigBA2 toxin-antitoxin complex from Vibrio cholerae. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 69(Pt 9), 1052-9. https://doi.org/10.1107/S1744309113021490

Crystallization of the HigBA2 toxin-antitoxin complex from Vibrio cholerae. / Hadǽi, San; Garcia-Pino, Abel; Martinez-Rodriguez, Sergio et al.

In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, Vol. 69, No. Pt 9, 09.2013, p. 1052-9.

Research output: Contribution to journal › Journal article › Research › peer-review

Hadǽi, S, Garcia-Pino, A, Martinez-Rodriguez, S, Verschueren, K, Christensen-Dalsgaard, M, Gerdes, K, Lah, J & Loris, R 2013, 'Crystallization of the HigBA2 toxin-antitoxin complex from Vibrio cholerae', Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, vol. 69, no. Pt 9, pp. 1052-9. https://doi.org/10.1107/S1744309113021490

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title = "Crystallization of the HigBA2 toxin-antitoxin complex from Vibrio cholerae",

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 {\AA}, and diffracted to 3.0 {\AA} 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 {\AA}. These crystals diffracted to 2.2 {\AA} 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 {\AA}, β = 106.7°, and diffracted to 1.8 {\AA} resolution.",

author = "San Hadǽi and Abel Garcia-Pino and Sergio Martinez-Rodriguez and Koen Verschueren and Mikkel Christensen-Dalsgaard and Kenn Gerdes and Jurij Lah and Remy Loris",

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T1 - Crystallization of the HigBA2 toxin-antitoxin complex from Vibrio cholerae

AU - Hadǽi, San

AU - Garcia-Pino, Abel

AU - Martinez-Rodriguez, Sergio

AU - Verschueren, Koen

AU - Christensen-Dalsgaard, Mikkel

AU - Gerdes, Kenn

AU - Lah, Jurij

AU - Loris, Remy

PY - 2013/9

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N2 - 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.

AB - 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.

U2 - 10.1107/S1744309113021490

DO - 10.1107/S1744309113021490

M3 - Journal article

C2 - 23989162

SN - 2053-230X

VL - 69

SP - 1052

EP - 1059

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

IS - Pt 9

ER -

Crystallization of the HigBA2 toxin-antitoxin complex from Vibrio cholerae

Abstract

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