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Purification, crystallization and preliminary X-ray analysis of a deletion mutant of a major buckwheat allergen.

ABSTRACT: A 16 kDa buckwheat protein (BWp16) is a major allergen responsible for immediate hypersensitivity reactions including anaphylaxis. A deletion mutant of BWp16 (rBWp16DeltaN) was overproduced and purified and was shown to be immunologically active. A three-wavelength MAD data set was collected from a crystal of selenomethionine-labelled rBWp16DeltaN. The crystal belonged to the triclinic space group P1, with unit-cell parameters a = 28.39, b = 31.54, c = 32.20 A, alpha = 111.92, beta = 108.91, gamma = 98.74 degrees . One monomer was expected to be present in the asymmetric unit based on the calculated Matthews coefficient of 1.76 A(3) Da(-1).

SUBMITTER: Kezuka Y

PROVIDER: S-EPMC2802877 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray analysis of a deletion mutant of a major buckwheat allergen.

Kezuka Yuichiro Y Itagaki Takashi T Satoh Rie R Teshima Reiko R Nonaka Takamasa T

Acta crystallographica. Section F, Structural biology and crystallization communications 20091127 Pt 12

A 16 kDa buckwheat protein (BWp16) is a major allergen responsible for immediate hypersensitivity reactions including anaphylaxis. A deletion mutant of BWp16 (rBWp16DeltaN) was overproduced and purified and was shown to be immunologically active. A three-wavelength MAD data set was collected from a crystal of selenomethionine-labelled rBWp16DeltaN. The crystal belonged to the triclinic space group P1, with unit-cell parameters a = 28.39, b = 31.54, c = 32.20 A, alpha = 111.92, beta = 108.91, gam ...[more]

PMID: 20054125

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