Crystallization and preliminary X-ray analysis of the Man(alpha1-2)Man-specific lectin from Bowringia mildbraedii in complex with its carbohydrate ligand.

TitleCrystallization and preliminary X-ray analysis of the Man(alpha1-2)Man-specific lectin from Bowringia mildbraedii in complex with its carbohydrate ligand.
Publication TypeJournal Article
Year of Publication2005
AuthorsGarcia-Pino, A., R. Loris, L. Wyns, and L. Buts
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
Volume61
IssuePt 10
Pagination931-4
Date Published2005 Oct 1
ISSN1744-3091
KeywordsAmino Acid Sequence, Animals, Carbohydrates, Chromatography, Affinity, Chromatography, Gel, Crystallization, Crystallography, X-Ray, Disaccharides, Fabaceae, Mannose, Mannosides, Models, Statistical, Molecular Sequence Data, Plant Lectins, Protein Conformation, Rabbits, Seeds, Sequence Homology, Amino Acid, Synchrotrons, Temperature, X-Rays
Abstract

The lectin from Bowringia mildbraedii seeds crystallizes in the presence of the disaccharide Man(alpha1-2)Man. The best crystals grow at 293 K within four weeks after a pre-incubation at 277 K to induce nucleation. A complete data set was collected to a resolution of 1.90 A using synchrotron radiation. The crystals belong to space group I222, with unit-cell parameters a = 66.06, b = 86.35, c = 91.76 A, and contain one lectin monomer in the asymmetric unit.

DOI10.1107/S174430910502854X
Alternate JournalActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
PubMed ID16511199
PubMed Central IDPMC1991310