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Preliminary crystallographic study of a complex between an heteroclitic anti-hen egg-white lysozyme antibody and the heterologous antigen pheasant egg-white lysozyme

Abstract : We report the preparation, crystallization and preliminary X-ray crystallographic study of the Fab fragment from a heteroclitic murine (BALB/c) monoclonal anti-hen egg-white lysozyme antibody complexed with a heterologous antigen, pheasant lysozyme. The complex between the heterologous antigen and the antibody has been crystallized from polyethylene glycol 8000 solutions in a form suitable for X-ray crystallographic studies. The crystals are monoclinic, space group C2 with a = 158.2 A, b = 49.1 A, c = 177.6 A, beta = 92.0 degrees (1 A = 0.1 nm).
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Submitted on : Tuesday, February 9, 2021 - 4:52:53 PM
Last modification on : Monday, March 1, 2021 - 11:25:12 AM

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Véronique Guillon, Pedro Alzari, Roberto Poljak. Preliminary crystallographic study of a complex between an heteroclitic anti-hen egg-white lysozyme antibody and the heterologous antigen pheasant egg-white lysozyme. Journal of Molecular Biology, Elsevier, 1987, 197 (2), pp.375-376. ⟨10.1016/0022-2836(87)90132-x⟩. ⟨pasteur-03136412⟩

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