Crystallization and preliminary x-ray investigation at 2.0 Å resolution of Bet v 1, a birch pollen protein causing IgE-mediated allergy
✍ Scribed by Spangfort, Michael D.; Larsen, Jørgen N.; Gajhede, Michael
- Book ID
- 101228432
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 318 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0887-3585
No coin nor oath required. For personal study only.
✦ Synopsis
The 17 kDa protein from Betula uemcosu (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 Escherichiu 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, X-rays from a rotating anode.