Volume 58, Issue 7 pp. 1246-1248

Crystallization and preliminary structural analysis of an antibody complex formed with PfMSP1-19, a malaria vaccine candidate

J. C. Pizarro

J. C. Pizarro

Unité d'Immunologie Structurale, CNRS URA 2185, Institut Pasteur, 25 Rue du Dr Roux, 75724 Paris, France

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V. Chitarra

V. Chitarra

Unité d'Immunologie Structurale, CNRS URA 2185, Institut Pasteur, 25 Rue du Dr Roux, 75724 Paris, France

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C. Calvet

C. Calvet

Unité d'Immunologie Structurale, CNRS URA 2185, Institut Pasteur, 25 Rue du Dr Roux, 75724 Paris, France

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D. Verger

D. Verger

Unité d'Immunologie Structurale, CNRS URA 2185, Institut Pasteur, 25 Rue du Dr Roux, 75724 Paris, France

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G. A. Bentley

G. A. Bentley

Unité d'Immunologie Structurale, CNRS URA 2185, Institut Pasteur, 25 Rue du Dr Roux, 75724 Paris, France

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First published: 15 June 2004
G. A. Bentley, e-mail: [email protected]

Abstract

The 11 kDa C-terminal fragment of the proteolyticly matured surface antigen, PfMSP1, from Plasmodium falciparum is a promising malaria vaccine candidate. The soluble recombinant form of this naturally occurring fragment has been crystallized as a complex with the Fab of a specific murine monoclonal antibody. The crystals belong to the space group P21, with unit-cell parameters a = 51.8, b = 213.5,c = 60.0 Å, β =101.0°, and with Z = 4. Diffraction data have been measured to 2.9 Å resolution and a preliminary model of the complex has been determined by molecular replacement. The epitope recognised by G17.12 is located on the N-terminal EGF-like domain of the antigen.

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