Open AccessPurification, crystallization and initial crystallographic characterization of peanut major allergen Ara h 3
Author(s) -
Jin Tengchuan,
Howard Andrew,
Zhang YuZhu
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107041176
Subject(s) - crystallization , storage protein , size exclusion chromatography , allergen , chemistry , legumin , chromatography , crystallography , organic chemistry , biochemistry , biology , allergy , immunology , enzyme , gene
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.