Crystallization and preliminary X-ray crystallographic studies of a lectin from the mushroom Marasmius oreades
Journal article, 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.

high-affinity

crystal-structure

gal-alpha-1

angstrom

protein

3gal

Author

E. Grahn

University of Gothenburg

Åsa Holmner

Chalmers University of Technology

C Cronet

Goteborgs Universitet

Chalmers University of Technology

Hiroaki Tateno

University Michigan Ann Arbor

Harry C. Winter

University Michigan Ann Arbor

Irwin J. Goldstein

University Michigan Ann Arbor

Ute Krengel

Chalmers, Department of Chemistry and Bioscience

Acta Crystallographica Section D: Biological Crystallography

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

Vol. 60 11 2038-2039

Subject Categories (SSIF 2011)

Inorganic Chemistry

Biochemistry and Molecular Biology

Biophysics

Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)

DOI

10.1107/S0907444904021183

More information

Created

10/6/2017