Published September 19, 2007 | Version v1
Journal article

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

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

Description

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

Availability note (English)

Available from http://dx.doi.org/10.1107/S1744309107041176; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2339721

Additional details

Publishing Information

Journal Title
Acta Crystallographica. Section F
Journal Volume
63
Journal Issue
Pt 10
Journal Page Range
p. 848-851
ISSN
1744-3091
CODEN
ACSFCL

INIS

Country of Publication
United Kingdom
Country of Input or Organization
International Atomic Energy Agency (IAEA)
INIS RN
46065679
Subject category
S75: CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY;
Descriptors DEI
CRYSTALLIZATION; DIFFUSION; GELS; IMPURITIES; INTERACTIONS; MATHEMATICAL SOLUTIONS; MONOCRYSTALS; PROTEINS; SOLUTIONS; VAPORS
Descriptors DEC
COLLOIDS; CRYSTALS; DISPERSIONS; FLUIDS; GASES; HOMOGENEOUS MIXTURES; MIXTURES; ORGANIC COMPOUNDS; PHASE TRANSFORMATIONS

Optional Information

Copyright
Copyright (c) International Union of Crystallography 2007
Notes
PMCID: PMC2339721; PMID: 17909286; PUBLISHER-ID: bw5210; OAI: oai:pubmedcentral.nih.gov:2339721