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

Cerrone Cabanos; Hiroyuki Urabe; Taro Masuda; Mary Rose Tandang-Silvas; Shigeru Utsumi; Bunzo Mikami; Nobuyuki Maruyama

doi:10.1107/S1744309110029040

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

Cerrone Cabanos, Hiroyuki Urabe, Taro Masuda, Mary Rose Tandang-Silvas, Shigeru Utsumi, Bunzo Mikami, Nobuyuki Maruyama

Genomic Medicine

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

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 Å 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 Å, Β = 107.144°. Data were collected at the BL-38B1 station of SPring-8 (Hyogo, Japan).

Original language	English (US)
Pages (from-to)	1071-1073
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	66
Issue number	9
DOIs	https://doi.org/10.1107/S1744309110029040
State	Published - Sep 2010

Keywords

Ara h 1
peanut allergens

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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10.1107/S1744309110029040

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title = "Crystallization and preliminary X-ray analysis of the major peanut allergen Ara h 1 core region",

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 {\AA} 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 {\AA}, Β = 107.144°. Data were collected at the BL-38B1 station of SPring-8 (Hyogo, Japan).",

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T1 - Crystallization and preliminary X-ray analysis of the major peanut allergen Ara h 1 core region

AU - Cabanos, Cerrone

AU - Urabe, Hiroyuki

AU - Masuda, Taro

AU - Tandang-Silvas, Mary Rose

AU - Utsumi, Shigeru

AU - Mikami, Bunzo

AU - Maruyama, Nobuyuki

PY - 2010/9

Y1 - 2010/9

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AB - 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 Å 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 Å, Β = 107.144°. Data were collected at the BL-38B1 station of SPring-8 (Hyogo, Japan).

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KW - peanut allergens

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

Abstract

Keywords

ASJC Scopus subject areas

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