Crystallization and preliminary X-ray analysis of the major peanut allergen Ara h 1 core region

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Sep 1;66(Pt 9):1071-3. doi: 10.1107/S1744309110029040. Epub 2010 Aug 26.

Abstract

Peanuts contain some of the most potent food allergens known to date. Ara h 1 is one of the three major peanut allergens. As a first step towards three-dimensional structure elucidation, recombinant Ara h 1 core region was cloned, expressed in Escherichia coli and purified to homogeneity. Crystals were obtained using 0.1 M sodium citrate pH 5.6, 0.1 M NaCl, 15% PEG 400 as precipitant. The crystals diffracted to 2.25 A resolution using synchrotron radiation and belonged to the monoclinic space group C2, with unit-cell parameters a=156.521, b=88.991, c=158.971 A, beta=107.144 degrees. Data were collected at the BL-38B1 station of SPring-8 (Hyogo, Japan).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, Plant / chemistry*
  • Arachis / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Glycoproteins / chemistry*
  • Membrane Proteins
  • Plant Proteins / chemistry*

Substances

  • Antigens, Plant
  • Ara h 1 protein, Arachis hypogaea
  • Glycoproteins
  • Membrane Proteins
  • Plant Proteins