Ostermeier C, Essen L O, Michel H
Max-Planck-Institut für Biophysik, Frankfurt/Main, Germany.
Proteins. 1995 Jan;21(1):74-7. doi: 10.1002/prot.340210110.
The Fv fragment of a monoclonal antibody, 7E2 (IgG1, kappa, murine), which is directed against the integral membrane protein cytochrome c oxidase (EC 1.9.3.1) from Paracoccus denitrificans, was cloned and produced in Escherichia coli. Crystals suitable for high-resolution X-ray analysis were obtained by microdialysis under low salt conditions. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions of a = 51.51 A, b = 56.15 A, c = 99.86 A (1 A = 0.1 nm) and contain one Fv fragment per asymmetric unit. Using synchrotron radiation diffraction data were collected up to 1.28 A resolution. This high resolution is very unusual for a heterodimeric protein. The crystals should open the way for refining not only the atomic positions, but also for obtaining information about internal dynamics.
一种针对反硝化副球菌的整合膜蛋白细胞色素c氧化酶（EC 1.9.3.1）的单克隆抗体7E2（IgG1，κ链，鼠源）的Fv片段，在大肠杆菌中进行了克隆和表达。通过低盐条件下的微量透析获得了适合高分辨率X射线分析的晶体。这些晶体属于正交晶系空间群P2(1)2(1)2(1)，晶胞参数为a = 51.51 Å，b = 56.15 Å，c = 99.86 Å（1 Å = 0.1 nm），每个不对称单元包含一个Fv片段。利用同步辐射收集了分辨率高达1.28 Å的衍射数据。对于异二聚体蛋白来说，这种高分辨率非常罕见。这些晶体不仅为精确定位原子位置，也为获取有关内部动力学的信息开辟了道路。
