Characterization and crystallization of a recombinant IgE Fab fragment in complex with the bovine [beta]-lactoglobulin allergen

M. Niemi, J. Jänis, Sirpa Jylhä, J. M. Kallio, Nina Hakulinen, Marja-Leena Laukkanen, Kristiina Takkinen, Juha Rouvinen

    Research output: Contribution to journalArticleScientificpeer-review

    13 Citations (Scopus)

    Abstract

    A D1 Fab fragment containing the allergen-binding variable domains of the IgE antibody was characterized by ESI FT-ICR mass spectrometry and crystallized with bovine [beta]-lactoglobulin (BLG) using the hanging-drop vapour-diffusion method at 293 K. X-ray data suitable for structure determination were collected to 2.8 Å resolution using synchrotron radiation. The crystal belonged to the orthorhombic space group P212121, with unit-cell parameters a = 67.0, b = 100.6, c = 168.1 Å. The three-dimensional structure of the D1 Fab fragment-BLG complex will provide the first insight into IgE antibody-allergen interactions at the molecular level.
    Original languageEnglish
    Pages (from-to)25-28
    Number of pages4
    JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
    Volume64
    Issue number1
    DOIs
    Publication statusPublished - 2008
    MoE publication typeA1 Journal article-refereed

    Keywords

    • Antibodies
    • Food allergens
    • IgE
    • Mass spectrometry

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