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

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

    Jin T, Howard A, Zhang YZ.

    Source

    Department of Biology, Illinois Institute of Technology, Chicago, IL 60616, USA.

    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.

    PMID:
    17909286
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC2339721
    Free PMC Article

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