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

A 16 kDa buckwheat protein (BWp16) is a major allergen responsible for immediate hypersensitivity reactions including anaphylaxis. A deletion mutant of BWp16 (rBWp16ΔN) was overproduced and purified and was shown to be immunologically active. A three-wavelength MAD data set was collected from a crys...

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Autores principales: Kezuka, Yuichiro, Itagaki, Takashi, Satoh, Rie, Teshima, Reiko, Nonaka, Takamasa
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2802877/
https://www.ncbi.nlm.nih.gov/pubmed/20054125
http://dx.doi.org/10.1107/S1744309109043127
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author Kezuka, Yuichiro
Itagaki, Takashi
Satoh, Rie
Teshima, Reiko
Nonaka, Takamasa
author_facet Kezuka, Yuichiro
Itagaki, Takashi
Satoh, Rie
Teshima, Reiko
Nonaka, Takamasa
author_sort Kezuka, Yuichiro
collection PubMed
description A 16 kDa buckwheat protein (BWp16) is a major allergen responsible for immediate hypersensitivity reactions including anaphylaxis. A deletion mutant of BWp16 (rBWp16ΔN) 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 rBWp16ΔN. The crystal belonged to the triclinic space group P1, with unit-cell parameters a = 28.39, b = 31.54, c = 32.20 Å, α = 111.92, β = 108.91, γ = 98.74°. One monomer was expected to be present in the asymmetric unit based on the calculated Matthews coefficient of 1.76 Å(3) Da(−1).
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spelling pubmed-28028772010-01-14 Purification, crystallization and preliminary X-ray analysis of a deletion mutant of a major buckwheat allergen Kezuka, Yuichiro Itagaki, Takashi Satoh, Rie Teshima, Reiko Nonaka, Takamasa Acta Crystallogr Sect F Struct Biol Cryst Commun Crystallization Communications A 16 kDa buckwheat protein (BWp16) is a major allergen responsible for immediate hypersensitivity reactions including anaphylaxis. A deletion mutant of BWp16 (rBWp16ΔN) 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 rBWp16ΔN. The crystal belonged to the triclinic space group P1, with unit-cell parameters a = 28.39, b = 31.54, c = 32.20 Å, α = 111.92, β = 108.91, γ = 98.74°. One monomer was expected to be present in the asymmetric unit based on the calculated Matthews coefficient of 1.76 Å(3) Da(−1). International Union of Crystallography 2009-11-27 /pmc/articles/PMC2802877/ /pubmed/20054125 http://dx.doi.org/10.1107/S1744309109043127 Text en © Kezuka et al. 2009 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Crystallization Communications
Kezuka, Yuichiro
Itagaki, Takashi
Satoh, Rie
Teshima, Reiko
Nonaka, Takamasa
Purification, crystallization and preliminary X-ray analysis of a deletion mutant of a major buckwheat allergen
title Purification, crystallization and preliminary X-ray analysis of a deletion mutant of a major buckwheat allergen
title_full Purification, crystallization and preliminary X-ray analysis of a deletion mutant of a major buckwheat allergen
title_fullStr Purification, crystallization and preliminary X-ray analysis of a deletion mutant of a major buckwheat allergen
title_full_unstemmed Purification, crystallization and preliminary X-ray analysis of a deletion mutant of a major buckwheat allergen
title_short Purification, crystallization and preliminary X-ray analysis of a deletion mutant of a major buckwheat allergen
title_sort purification, crystallization and preliminary x-ray analysis of a deletion mutant of a major buckwheat allergen
topic Crystallization Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2802877/
https://www.ncbi.nlm.nih.gov/pubmed/20054125
http://dx.doi.org/10.1107/S1744309109043127
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