Crystallization and preliminary X-ray analysis of ginkbilobin-2 from Ginkgo biloba seeds: a novel antifungal protein with homology to the extracellular domain of plant cysteine-rich receptor-like kinases

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Sep 1;63(Pt 9):737-9. doi: 10.1107/S1744309107034793. Epub 2007 Aug 10.

Abstract

The antifungal protein ginkbilobin-2 (Gnk2) from Ginkgo biloba seeds does not show homology to other pathogenesis-related proteins, but does show homology to the extracellular domain of plant cysteine-rich receptor-like kinases. Native Gnk2 purified from ginkgo nuts and the selenomethionine derivative of recombinant Gnk2 (SeMet-rGnk2) were crystallized by the sitting-drop vapour-diffusion method using different precipitants. X-ray diffraction data were collected from Gnk2 at 2.38 A resolution and from SeMet-rGnk2 at 2.79 A resolution using a synchrotron-radiation source. The crystals of both proteins belonged to the primitive cubic space group P2(1)3, with unit-cell parameters a = b = c = 143.2 A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antimicrobial Cationic Peptides / chemistry*
  • Antimicrobial Cationic Peptides / isolation & purification
  • Crystallization
  • Cysteine
  • Ginkgo biloba
  • Plant Proteins / chemistry
  • Plant Proteins / isolation & purification
  • Plants / enzymology
  • Protein Kinases / chemistry
  • Protein Kinases / isolation & purification
  • Seeds / chemistry*
  • X-Ray Diffraction

Substances

  • Antimicrobial Cationic Peptides
  • Plant Proteins
  • ginkbilobin-2 protein, Ginkgo biloba
  • Protein Kinases
  • Cysteine