Crystallization and preliminary X-ray diffraction analysis of the lectin from Canavalia boliviana Piper seeds

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Mar 1;65(Pt 3):213-5. doi: 10.1107/S1744309109000797. Epub 2009 Feb 12.

Abstract

Plant lectins are the most studied group of carbohydrate-binding proteins. Despite the high similarity between the members of the Diocleinae subtribe (Leguminosae) group, they present differing biological activities. Canavalia boliviana lectin (Cbol) was purified using a Sephadex G-50 column and crystallized in the presence of X-Man by hanging-drop vapour diffusion at 293 K. After optimization, crystals suitable for diffraction were obtained under the condition 0.1 M HEPES pH 7.5 and 3.0 M sodium formate. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a = 126.70, b = 66.64, c = 64.99 A, alpha = 90.0, beta = 120.8, gamma = 90.0 degrees . Assuming the presence of a dimer in the asymmetric unit, the solvent content was estimated to be about 46%. A complete data set was collected at 1.5 A resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Canavalia / chemistry*
  • Chromatography, Affinity
  • Crystallization
  • Crystallography, X-Ray
  • Electrophoresis, Polyacrylamide Gel
  • Plant Lectins / analysis
  • Plant Lectins / chemistry*
  • Seeds / chemistry*

Substances

  • Plant Lectins
  • lectin, Canavalia