title: Crystallization and preliminary X-ray diffraction analysis of the human dimeric S-Lac lectin (L-14-II).
abstract: The human recombinant S-Lac lectin, L-14-II, produced in an Escherichia coli expression system, has been co-crystallized in the presence of lactose by the hanging drop vapor diffusion method. The crystals grow in space group P2(1)2(1)2(1) with unit cell dimensions of a = 43.6 A, b = 57.8 A, c = 108.2 A, with a dimer in the asymmetric unit. On a conventional rotating anode the crystals diffract to at least 2.8 A resolution.
authors.affiliation: Department of Molecular Genetics, University of Toronto, Ontario, Canada.
authors.forename: Y D
authors.initials: YD
authors.lastname: Lobsanov
authors.forename: M A
authors.initials: MA
authors.lastname: Gitt
authors.forename: H
authors.initials: H
authors.lastname: Leffler
authors.forename: S
authors.initials: S
authors.lastname: Barondes
authors.forename: J M
authors.initials: JM
authors.lastname: Rini
mesh_terms: D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D037161:Galectins; D006388:Hemagglutinins / Q000737:chemistry*; D006801:Humans; D037102:Lectins / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D037161:Galectins; D006388:Hemagglutinins; D037102:Lectins; D011994:Recombinant Proteins