Purification, crystallization and initial crystallographic characterization of peanut major allergen Ara h 3

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Oct 1;63(Pt 10):848-51. doi: 10.1107/S1744309107041176. Epub 2007 Sep 19.

Abstract

The peanut is a significant food source, but is responsible for many cases of anaphylaxis. The peanut 11S legumin-like seed storage protein Ara h 3 is one of the best characterized allergens. In this study, Ara h 3 was extracted from peanut kernels and purified by sequential anion-exchange, hydrophobic interaction and gel-filtration chromatography to very high purity to facilitate crystallization and structural studies. Well diffracting single crystals were obtained by the vapor-diffusion method. A molecular-replacement structural solution has been obtained and refinement of the structure is currently under way.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Allergens / chemistry*
  • Allergens / isolation & purification*
  • Antigens, Plant
  • Arachis / chemistry
  • Arachis / immunology*
  • Base Sequence
  • Crystallization
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Plant Extracts / chemistry
  • Protein Structure, Secondary
  • Seed Storage Proteins

Substances

  • Allergens
  • Antigens, Plant
  • Plant Extracts
  • Seed Storage Proteins
  • allergen Ara h3