title: Crystallization and preliminary X-ray diffraction studies of antigen--antibody complexes.
abstract: Monoclonal antibodies of predefined specificity have been purified and crystallized as single components or complexed with their specific antigens. The intersegmental flexibility of antibody molecules has imposed the strategy of attempting to crystallize their Fab fragments separately. Intrasegmental mobility in Fabs has rarely been an obstacle to their crystallization. The immune system, however, provides a large functional and structural diversity of antibody molecules suitable for crystallization and X-ray diffraction studies.
authors.affiliation: Department of Immunology, Institut Pasteur, Paris, France.
authors.forename: V
authors.initials: V
authors.lastname: Chitarra-Guillon
authors.forename: H
authors.initials: H
authors.lastname: Souchon
authors.forename: G
authors.initials: G
authors.lastname: Boulot
authors.forename: M M
authors.initials: MM
authors.lastname: Riottot
authors.forename: R
authors.initials: R
authors.lastname: Mariuzza
authors.forename: D
authors.initials: D
authors.lastname: Tello
authors.forename: R J
authors.initials: RJ
authors.lastname: Poljak
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000918:Antibody Specificity; D000936:Antigen-Antibody Complex / Q000302:isolation & purification*; D003460:Crystallization; D007140:Immunoglobulin Fab Fragments / Q000302:isolation & purification; D051379:Mice; D009113:Muramidase / Q000276:immunology; D014961:X-Ray Diffraction
chemical_list: D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D007140:Immunoglobulin Fab Fragments; D009113:Muramidase