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Crystallization and preliminary x‐ray investigation at 2.0 Å resolution of Bet v 1, a birch pollen protein causing IgE‐mediated allergy
Author(s) -
Spangfort Michael D.,
Larsen Jørgen N.,
Gajhede Michael
Publication year - 1996
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199611)26:3<358::aid-prot10>3.0.co;2-n
Subject(s) - pollen , orthorhombic crystal system , escherichia coli , immunoglobulin e , recombinant dna , resolution (logic) , allergen , chemistry , allergy , biology , crystallography , botany , biochemistry , crystal structure , immunology , antibody , gene , artificial intelligence , computer science
The 17 kDa protein from Betula verrucosa (White Birch) pollen, Bet v 1, is the clinically most important birch pollen allergen causing immediate Type I IgE‐mediated allergy. The three‐dimensional structure of Bet v 1 and its IgE‐binding epitopes are at present not known. In addition, the biological function of Bet v 1 in birch pollen is not fully established. In this work, Bet v 1 has been expressed in Escherichia coli as a recombinant protein, purified and crystallized. The space group of recombinant Bet v 1 crystals is orthorhombic C2221 with unit cell parameters a = 32.13 Å, b = 74.22 Å, and c = 118.60 Å. There is one Bet v 1 molecule per asymmetric unit and the water content is 41%. Crystals diffract to 2.0 Å resolution and a complete native data set was collected from a single crystal using CuK α X‐rays from a rotating anode. © 1996 Wiley‐Liss, Inc.