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. 2009 Dec 1;65(Pt 12):1267-70.
doi: 10.1107/S1744309109043127. Epub 2009 Nov 27.

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

Affiliations

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

Yuichiro Kezuka et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

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).

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Figures

Figure 1
Figure 1
Crystals of rBWp16ΔN (a) and its SeMet derivative (b). The scale bars correspond to 0.1 mm. The crystals in (a) and (b) were obtained under conditions I and II, respectively.
Figure 2
Figure 2
A section at w = 0.317 of the anomalous difference Patterson map for the SeMet derivative containing the highest peak. The map was calculated using the peak data and is contoured at intervals of 0.5σ starting at 3.0σ above the mean density level.

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