Abstract
Diffraction-quality crystals have been obtained for complexes of each of the major wheat germ agglutinin (WGA) isolectins with the tryptic sialoglycopeptide T-5 from the WGA red cell receptor glycophorin A. This octa-glycopeptide possesses a Thr-linked carbohydrate moiety (GalNAc(NeuNAc)-Gal-NeuNAc) with specificity for the WGA binding site. The crystals belong to the orthorhombic space group P2 12 12 and have unit cell dimensions: a =112.2 A ̊ , b = 51.0 A ̊ , c = 63.5 A ̊ (isolectin 1); a = 109.0 A ̊ , b = 52.3 A ̊ , c = 62.4 A ̊ (isolectin 2). There are two monomer complexes in each asymmetric unit.
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