Purification, crystallization and preliminary X-ray studies of sylvaticin, an elicitin-like protein from Pythium sylvaticum

Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):362-4. doi: 10.1107/S090744490302777X. Epub 2004 Jan 23.

Abstract

Sylvaticin belongs to the elicitin family. These 10 kDa oomycetous proteins induce a hypersensitive response in plants, including necrosis and cell death, but subsequently leading to a non-specific systemic acquired resistance (SAR) against other pathogens. Sylvaticin has been crystallized using PEG 2000 MME as a precipitant agent in the presence of nickel chloride. The crystals belong to space group C2, with unit-cell parameters a = 99.29, b = 25.67, c = 67.45 A, beta = 99.66 degrees. Diffraction data were recorded to 2.1 A resolution at a synchrotron-radiation source.

MeSH terms

  • Algal Proteins / chemistry*
  • Crystallography, X-Ray
  • Furans / chemistry*
  • Furans / isolation & purification
  • Nickel / chemistry
  • Polyethylene Glycols / chemistry
  • Protein Conformation
  • Proteins
  • Pythium / metabolism*
  • Solvents / chemistry
  • Synchrotrons

Substances

  • Algal Proteins
  • Furans
  • Proteins
  • Solvents
  • elicitin, Phytophthora
  • sylvaticin
  • Polyethylene Glycols
  • nickel chloride
  • Nickel