Open AccessPurification, crystallization and preliminary X‐ray analysis of a deletion mutant of a major buckwheat allergen
Author(s) -
Kezuka Yuichiro,
Itagaki Takashi,
Satoh Rie,
Teshima Reiko,
aka Takamasa
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109043127
Subject(s) - allergen , triclinic crystal system , mutant , monomer , crystallization , chemistry , microbiology and biotechnology , crystal (programming language) , crystallography , crystal structure , biology , allergy , biochemistry , immunology , organic chemistry , gene , computer science , programming language , polymer
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 P 1, 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 .