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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jan 1;64(Pt 1):25-8. Epub 2007 Dec 20.

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

Author information

1
Department of Chemistry, University of Joensuu, PO Box 111, FIN-80101 Joensuu, Finland. merja.niemi@joensuu.fi

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.

PMID:
18097096
PMCID:
PMC2373997
DOI:
10.1107/S174430910706160X
[Indexed for MEDLINE]
Free PMC Article

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