Nyborg J, Kjeldgaard M
Department of Molecular and Structural Biology, University of Aarhus, Denmark.
Curr Opin Biotechnol. 1996 Aug;7(4):369-75. doi: 10.1016/s0958-1669(96)80110-8.
The past year has brought some notable advances in our understanding of the structure and function of elongation factors (EFs) involved in protein biosynthesis. The structures of the ternary complex of aminoacylated tRNA with EF-Tu.GTP and of the complex EF-Tu.EF-Ts have been determined. Within the same period, new cryo-electron microscopy reconstructions of ribosome particles have been obtained.
在过去的一年里，我们对参与蛋白质生物合成的延伸因子（EFs）的结构和功能有了一些显著的认识进展。已确定了氨酰化tRNA与EF-Tu.GTP的三元复合物以及EF-Tu.EF-Ts复合物的结构。在同一时期，还获得了核糖体颗粒的新低温电子显微镜重建图像。
