Preliminary crystallographic study of a complex between an heteroclitic anti-hen egg-white lysozyme antibody and the heterologous antigen pheasant egg-white lysozyme.
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).
Guillon
V
V
Institut Pasteur Département d'Immunologie, Paris, France.
Alzari
P M
PM
Poljak
R J
RJ
D000818:Animals; D000936:Antigen-Antibody Complex / Q000276:immunology*; D001717:Birds; D003461:Crystallography; D007140:Immunoglobulin Fab Fragments / Q000276:immunology; D009113:Muramidase / Q000276:immunology*
D000936:Antigen-Antibody Complex; D007140:Immunoglobulin Fab Fragments; D009113:Muramidase