Crystallization and Preliminary Crystallographic Analysis of a Tetrameric Isolectin from Vicia villosa, Specific for the Tn Antigen

Jean-Luc Eiselé (1) , Diana Tello (2) , Eduardo Osinaga (3) , Alberto Roseto (3) , Pedro M. Alzari (2)

1 Neurobiologie moléculaire
2 Immunobiologie
3 Division d'immunocytologie appliquée [Compiègne]

Isolectin B4 isolated from Vicia villosa seeds is specific for the Tn antigen, a carcinoma-associated molecular marker. Crystals of the isolectin grown in the presence of carbohydrate are tetragonal, space group P 41 (or P43), with a = 91·3 Å, c = 151·7 Å and one tetramer in the asymmetric unit. The crystals diffract X-rays to 2·8 Å resolution and are suitable for high-resolution structural analysis.

Keywords: plant lectin; Tn antigen; X-ray crystallography; Vicia villosa; crystallization

Domains: Cristallography; Structural Biology [q-bio.BM]; Biochemistry, Molecular Biology; Bioinformatics [q-bio.QM]; Biological Physics [physics.bio-ph]; Cellular Biology

Jean-Luc Eiselé, Diana Tello, Eduardo Osinaga, Alberto Roseto, Pedro M. Alzari. Crystallization and Preliminary Crystallographic Analysis of a Tetrameric Isolectin from Vicia villosa, Specific for the Tn Antigen. Journal of Molecular Biology, 1993, 230 (2), pp.670-672. ⟨10.1006/jmbi.1993.1180⟩. ⟨pasteur-03136511⟩