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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...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
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International Union of Crystallography
2009
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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). |
format | Text |
id | pubmed-2802877 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
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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