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

Purification, crystallization and initial crystallographic characterization of peanut major... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

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

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References (9)

Publisher
Wiley
Copyright
Copyright © 2007 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309107041176
pmid
17909286
Publisher site
See Article on Publisher Site

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.

Journal

Acta Crystallographica Section FWiley

Published: Oct 1, 2007

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