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

Abstract

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.

Authors:
; ;  [1]
  1. Department of Biology, Illinois Institute of Technology, Chicago, IL 60616 (United States)
Publication Date:
OSTI Identifier:
22360399
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 63; Journal 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); Journal ID: ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; DIFFUSION; GELS; IMPURITIES; INTERACTIONS; MATHEMATICAL SOLUTIONS; MONOCRYSTALS; PROTEINS; SOLUTIONS; VAPORS

Citation Formats

Jin, Tengchuan, Howard, Andrew, and Zhang, Yu-Zhu, E-mail: zhangy@iit.edu. Purification, crystallization and initial crystallographic characterization of peanut major allergen Ara h 3. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107041176.
Jin, Tengchuan, Howard, Andrew, & Zhang, Yu-Zhu, E-mail: zhangy@iit.edu. Purification, crystallization and initial crystallographic characterization of peanut major allergen Ara h 3. United Kingdom. doi:10.1107/S1744309107041176.
Jin, Tengchuan, Howard, Andrew, and Zhang, Yu-Zhu, E-mail: zhangy@iit.edu. Mon . "Purification, crystallization and initial crystallographic characterization of peanut major allergen Ara h 3". United Kingdom. doi:10.1107/S1744309107041176.
@article{osti_22360399,
title = {Purification, crystallization and initial crystallographic characterization of peanut major allergen Ara h 3},
author = {Jin, Tengchuan and Howard, Andrew and Zhang, Yu-Zhu, E-mail: zhangy@iit.edu},
abstractNote = {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.},
doi = {10.1107/S1744309107041176},
journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 10,
volume = 63,
place = {United Kingdom},
year = {2007},
month = {10}
}