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Epitope Mapping Protocols pp 11–23Cite as

Crystallographic Studies of Antigen-Antibody Interactions

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Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 66))

Abstract

X-ray crystallography provides a powerful tool for the study of antigen- antibody interactions. Information provided by crystallographic studies of antigen-antibody complexes includes the topological description of intermolecular contacts and the nature of interactions between amino acid residues. In cases where structures of both liganded and unliganded forms of an antigen or antibody fragment are known, crystallographic studies have led to a more dynamic view of binding, often showing conformational changes (induced fit) in the antibody or antigen and displacement of water molecules at the binding interface.

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Author information

Authors and Affiliations

  1. Unité d’Immunologie Structurale, Institut Pasteur, Paris, France

    Frederick A. Saul & Pedro M. Alzari

Authors
  1. Frederick A. Saul
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  2. Pedro M. Alzari
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Editor information

Editors and Affiliations

  1. The North East Wales Institute, Wrexham, UK

    Glenn E. Morris

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© 1996 Humana Press Inc.

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Saul, F.A., Alzari, P.M. (1996). Crystallographic Studies of Antigen-Antibody Interactions. In: Morris, G.E. (eds) Epitope Mapping Protocols. Methods in Molecular Biology™, vol 66. Humana Press. https://doi.org/10.1385/0-89603-375-9:11

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  • DOI: https://doi.org/10.1385/0-89603-375-9:11

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-375-7

  • Online ISBN: 978-1-59259-552-5

  • eBook Packages: Springer Protocols

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