Open AccessCharacterization and crystallization of a recombinant IgE Fab fragment in complex with the bovine β‐lactoglobulin allergen
Author(s) -
Niemi Merja,
Jänis Janne,
Jylhä Sirpa,
Kallio Johanna M.,
Hakulinen Nina,
Laukkanen MarjaLeena,
Takkinen Kristiina,
Rouvinen Juha
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910706160x
Subject(s) - allergen , orthorhombic crystal system , chemistry , immunoglobulin e , recombinant dna , crystallization , mass spectrometry , antibody , crystal structure , crystallography , chromatography , allergy , biochemistry , immunology , organic chemistry , biology , gene
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 β‐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 P 2 1 2 1 2 1 , 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.