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

Journal Article · Mon Oct 01 00:00:00 EDT 2007 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309107041176· OSTI ID:22360399

Jin, Tengchuan; Howard, Andrew; Zhang, Yu-Zhu ^[1]

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1. Department of Biology, Illinois Institute of Technology, Chicago, IL 60616 (United States)

The crystallization of peanut allergen Ara h 3 is reported. 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.

• OSTI ID: 22360399
• Journal Information: Acta Crystallographica. Section F, Vol. 63, Issue Pt 10; Other Information: PMCID: PMC2339721; PMID: 17909286; PUBLISHER-ID: bw5210; OAI: oai:pubmedcentral.nih.gov:2339721; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
DIFFUSION
GELS
IMPURITIES
INTERACTIONS
MATHEMATICAL SOLUTIONS
MONOCRYSTALS
PROTEINS
SOLUTIONS
VAPORS