title: Crystallization and preliminary X-ray investigation at 2.0 A resolution of Bet v 1, a birch pollen protein causing IgE-mediated allergy.
abstract: 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 A, b = 74.22 A, and c = 118.60 A. There is one Bet v 1 molecule per asymmetric unit and the water content is 41%. Crystals diffract to 2.0 A resolution and a complete native data set was collected from a single crystal using CuK alpha X-rays from a rotating anode.
authors.affiliation: ALK A/S, Research Department, Hørsholm, Denmark.
authors.forename: M D
authors.initials: MD
authors.lastname: Spangfort
authors.forename: J N
authors.initials: JN
authors.lastname: Larsen
authors.forename: M
authors.initials: M
authors.lastname: Gajhede
mesh_terms: D000485:Allergens / Q000737:chemistry* / Q000235:genetics; D052179:Antigens, Plant; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D006967:Hypersensitivity / Q000276:immunology; D007073:Immunoglobulin E / Q000276:immunology; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics; D011058:Pollen / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D014197:Trees / Q000737:chemistry
chemical_list: D000485:Allergens; D052179:Antigens, Plant; D010940:Plant Proteins; D011994:Recombinant Proteins; C061312:Bet v 1 allergen, Betula; D007073:Immunoglobulin E