Crystallization and preliminary X-ray analysis of the major peanut allergen Ara h 1 core region.
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).
Cabanos
Cerrone
C
Laboratory of Food Quality Design and Development, Graduate School of Agriculture, Kyoto University, Uji, Kyoto, Japan.
Urabe
Hiroyuki
H
Masuda
Taro
T
Tandang-Silvas
Mary Rose
MR
Utsumi
Shigeru
S
Mikami
Bunzo
B
Maruyama
Nobuyuki
N
D052179:Antigens, Plant / Q000737:chemistry*; D010367:Arachis / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006023:Glycoproteins / Q000737:chemistry*; D008565:Membrane Proteins; D010940:Plant Proteins / Q000737:chemistry*
D052179:Antigens, Plant; C500889:Ara h 1 protein, Arachis hypogaea; D006023:Glycoproteins; D008565:Membrane Proteins; D010940:Plant Proteins
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