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Crystallization and preliminary X-ray diffraction data of the Fab fragment of a monoclonal antibody against apamin, a bee venom neurotoxin

Christiane Devaux 1 Maria-Léria Defendini Pedro Alzar 2 Chantal Abergel 3 Claude Granier Juan Fontecilla-Camps 3
1 Laboratoire de biochimie [Marseille]
2 Immunologie structurale
3 Laboratoire de Cristallographie et de Cristallisation des Macromolécules Biologiques [Marseille]
Abstract : Fab fragments of anti-apamin monoclonal antibodies have been purified to homogeneity and crystallized. The crystals belong to the monoclinic space group P21 with cell dimensions a = 99.0 +/- 0.3 A, b = 137.1 +/- 0.4 A, c = 76.0 +/- 0.2 A and beta = 92.9 +/- 0.9 degrees. They most likely contain four molecules in the asymmetric unit (Vm = 2.39 A3/Da). The possibility of the existence of non-crystallographic symmetry is discussed.
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https://hal-pasteur.archives-ouvertes.fr/pasteur-03136481
Contributor : Marie de Tarragon <>
Submitted on : Tuesday, February 9, 2021 - 5:14:30 PM
Last modification on : Friday, April 2, 2021 - 11:36:00 AM

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Christiane Devaux, Maria-Léria Defendini, Pedro Alzar, Chantal Abergel, Claude Granier, et al.. Crystallization and preliminary X-ray diffraction data of the Fab fragment of a monoclonal antibody against apamin, a bee venom neurotoxin. FEBS Letters, Wiley, 1991, 286 (1-2), pp.64-66. ⟨10.1016/0014-5793(91)80941-u⟩. ⟨pasteur-03136481⟩

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