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

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 A resolution using synchrotron radiation. The crystal belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 67.0, b = 100.6, c = 168.1 A. 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.

SUBMITTER: Niemi M

PROVIDER: S-EPMC2373997 | biostudies-literature | 2008 Jan

REPOSITORIES: biostudies-literature

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

Niemi Merja M Jänis Janne J Jylhä Sirpa S Kallio Johanna M JM Hakulinen Nina N Laukkanen Marja-Leena ML Takkinen Kristiina K Rouvinen Juha J

Acta crystallographica. Section F, Structural biology and crystallization communications 20071220 Pt 1

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 A resolution using synchrotron radiation. The crystal belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 67.0, b = 100.6, c = 168.1 A. The three-di ...[more]

PMID: 18097096

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