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

Journal Article · Tue Jan 01 04:00:00 EST 2008 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S174430910706160X· OSTI ID:22360467

Niemi, Merja; Jänis, Janne ^[1]; Jylhä, Sirpa ^[2]; Kallio, Johanna M.; Hakulinen, Nina ^[1]; Laukkanen, Marja-Leena; Takkinen, Kristiina ^[2]; Rouvinen, Juha ^[1]

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1. Department of Chemistry, University of Joensuu, PO Box 111, FIN-80101 Joensuu (Finland)
2. VTT Technical Research Centre of Finland, PO Box 1000, FIN-02044 VTT (Finland)

The high-resolution mass-spectrometric characterization, crystallization and X-ray diffraction studies of a recombinant IgE Fab fragment in complex with bovine β-lactoglobulin are reported. 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 P2{sub 1}2{sub 1}2{sub 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.

• OSTI ID: 22360467
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 1 Vol. 64; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
ANTIBODIES
CATTLE
CRYSTALLIZATION
CRYSTALS
DIFFUSION
INTERACTIONS
MASS SPECTROSCOPY
RESOLUTION
SPACE GROUPS
SYNCHROTRON RADIATION
X-RAY DIFFRACTION