Spangfort M D, Larsen J N, Gajhede M
ALK A/S, Research Department, Hørsholm, Denmark.
Proteins. 1996 Nov;26(3):358-60. doi: 10.1002/(SICI)1097-0134(199611)26:3<358::AID-PROT10>3.0.CO;2-N.
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.
疣枝桦（白桦）花粉中的17 kDa蛋白Bet v 1是临床上最重要的桦树花粉过敏原，可引发I型IgE介导的速发型过敏反应。目前尚不清楚Bet v 1的三维结构及其IgE结合表位。此外，Bet v 1在桦树花粉中的生物学功能也尚未完全明确。在本研究中，Bet v 1已在大肠杆菌中作为重组蛋白表达、纯化并结晶。重组Bet v 1晶体的空间群为正交晶系C2221，晶胞参数a = 32.13 Å，b = 74.22 Å，c = 118.60 Å。每个不对称单元中有一个Bet v 1分子，含水量为41%。晶体衍射分辨率为2.0 Å，使用旋转阳极产生的CuKα X射线从一块单晶收集到了完整的天然数据集。
