CRYSTALLIZATION AND PRELIMINARY-X-RAY INVESTIGATION AT 2.0 ANGSTROM RESOLUTION OF BET-V-1, A BIRCH POLLEN PROTEIN CAUSING IGE-MEDIATED ALLERGY

The 17 kDa protein from Betula verrucosa (White Birch) pollen, Bet v 1 , is the clinically most important birch pollen allergen causing immed iate Type I IgE-mediated allergy, The three-dimensional structure of B et v 1 and its IgE-binding epitopes are at present not known. In addit ion, the biological function of Bet v 1 in birch pollen is not fully e stablished, In this work, Bet v 1 has been expressed in Escherichia co li as a recombinant protein, purified and crystallized. The space grou p of recombinant Bet v 1 crystals is orthorhombic C2221 with unit cell parameters a = 32.13 Angstrom, b = 74.22 Angstrom, and c = 118.60 Ang strom. There is one Bet v 1 molecule per asymmetric unit and the water content is 41%, Crystals diffract to 2.0 Angstrom resolution and a co mplete native data set was collected from a single crystal using CuKal pha X-rays from a rotating anode. (C) 1996 Wiley-Liss, Inc.