Delbaere L T, Vandonselaar M, Quail J W, Waygood E B, Lee J S
Department of Biochemistry, University of Saskatchewan, Saskatoon, Canada.
J Biol Chem. 1989 Nov 5;264(31):18645-6.
Single crystals of the complex of a monoclonal Fab fragment with the histidine-containing protein of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli have been grown. This represents one of the first Fab-protein antigen complexes in which the same Fab fragment has previously been crystallized in the uncomplexed state and the structure solved (Prasad, L., Vandonselaar, M., Lee, J. S., and Delbaere, L. T. J. (1988) J. Biol. Chem. 263, 2571-2574). Single crystals up to 0.25 x 0.50 x 0.05 mm in size were grown by the technique of washing and reseeding. The space group is C2, with unit cell dimensions a = 130.0, b = 68.1, and c = 77.6 A; beta = 97.3 degrees; and Z = 4. There is one Fab-histidine-containing protein complex/asymmetric unit, and the solvent content is estimated to be 57%.
已培养出单克隆Fab片段与大肠杆菌磷酸烯醇丙酮酸：糖磷酸转移酶系统中含组氨酸蛋白的复合物的单晶。这是最早的Fab - 蛋白质抗原复合物之一，其中相同的Fab片段先前已在未复合状态下结晶并解析了结构（Prasad, L., Vandonselaar, M., Lee, J. S., and Delbaere, L. T. J. (1988) J. Biol. Chem. 263, 2571 - 2574）。通过洗涤和再接种技术培养出了尺寸达0.25×0.50×0.05 mm的单晶。空间群为C2，晶胞参数a = 130.0，b = 68.1，c = 77.6 Å；β = 97.3°；Z = 4。每个不对称单元中有一个Fab - 含组氨酸蛋白复合物，溶剂含量估计为57%。
