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Crystallization and preliminary X-ray analysis of the major peanut allergen Ara h 1 core region.

Authors :
Cabanos C
Urabe H
Masuda T
Tandang-Silvas MR
Utsumi S
Mikami B
Maruyama N
Source :
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2010 Sep 01; Vol. 66 (Pt 9), pp. 1071-3. Date of Electronic Publication: 2010 Aug 26.
Publication Year :
2010

Abstract

Peanuts contain some of the most potent food allergens known to date. Ara h 1 is one of the three major peanut allergens. As a first step towards three-dimensional structure elucidation, recombinant Ara h 1 core region was cloned, expressed in Escherichia coli and purified to homogeneity. Crystals were obtained using 0.1 M sodium citrate pH 5.6, 0.1 M NaCl, 15% PEG 400 as precipitant. The crystals diffracted to 2.25 A resolution using synchrotron radiation and belonged to the monoclinic space group C2, with unit-cell parameters a=156.521, b=88.991, c=158.971 A, beta=107.144 degrees. Data were collected at the BL-38B1 station of SPring-8 (Hyogo, Japan).

Details

Language :
English
ISSN :
1744-3091
Volume :
66
Issue :
Pt 9
Database :
MEDLINE
Journal :
Acta crystallographica. Section F, Structural biology and crystallization communications
Publication Type :
Academic Journal
Accession number :
20823529
Full Text :
https://doi.org/10.1107/S1744309110029040