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Title: Crystallization and preliminary X-ray analysis of the major peanut allergen Ara h 1 core region.
Authors: Cabanos, Cerrone  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0001-5915-3683 (unconfirmed)
Urabe, Hiroyuki
Masuda, Taro  kyouindb  KAKEN_id
Tandang-Silvas, Mary Rose
Utsumi, Shigeru
Mikami, Bunzo  kyouindb  KAKEN_id
Maruyama, Nobuyuki  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0002-1369-9629 (unconfirmed)
Author's alias: 丸山, 伸之
Keywords: peanut allergens
Ara h 1
Issue Date: 1-Sep-2010
Publisher: International Union of Crystallography
Journal title: Acta crystallographica. Section F, Structural biology and crystallization communications
Volume: 66
Issue: Pt 9
Start page: 1071
End page: 1073
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).
Rights: © International Union of Crystallography
URI: http://hdl.handle.net/2433/131796
DOI(Published Version): 10.1107/S1744309110029040
PubMed ID: 20823529
Appears in Collections:Journal Articles

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