Crystallization and preliminary X-ray crystallographic studies of a lectin from the mushroom Marasmius oreades
Artikel i vetenskaplig tidskrift, 2004

The Marasmius oreades agglutinin (MOA) recognizes blood group B oligosaccharides. This mushroom lectin belongs to the ricin superfamily and is currently the only lectin known with exclusive specificity for Galα1,3Gal-structures, as occur in the subterminally fucosylated blood group B epitope Galα1,3(Fucα1,2)Galβ1,4GlcNAc (MOA's preferred ligand) or without fucosylation in the xenotransplantation epitope. MOA has been co-crystallized with the linear blood group B trisaccharide Galα1,3Galβ1,4GlcNAc using the hanging-drop vapour-diffusion technique at room temperature. MOA crystals were grown in the presence of ammonium formate and HEPES buffer. A 3.0 Å data set has been collected. Preliminary analysis of the X-ray data is consistent with space group P3 1 or P3 2 and unit-cell parameters a = b = 105, c = 113 Å, with two dimers per asymmetric unit. © 2004 International Union of Crystallography.

gal-alpha-1

protein

high-affinity

angstrom

3gal

crystal-structure

Författare

E. Grahn

Göteborgs universitet

Åsa Holmner

Chalmers University of Technology

C Cronet

Chalmers University of Technology

Göteborgs universitet

Hiroaki Tateno

University of Michigan

Harry C. Winter

University of Michigan

Irwin J. Goldstein

University of Michigan

Ute Krengel

Chalmers, Institutionen för kemi och biovetenskap

Acta Crystallographica Section D: Biological Crystallography

0907-4449 (ISSN) 1399-0047 (eISSN)

Vol. 60 11 2038-2039

Ämneskategorier

Oorganisk kemi

Biokemi och molekylärbiologi

Biofysik

Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci)

DOI

10.1107/S0907444904021183