《生命科学》 2010, 22(3): 252-255
摘 要:
摘 要:单颗粒电镜结合其他方法能够在(近)原子水平提供结构模型,已经成为一种研究大蛋白复合物的有效方法。该文将以两个大的蛋白裂解复合物——tripeptidyl peptidase II (6 MDa)和26S蛋白酶体(2.5 MDa)举例说明。低温电子层析能进行非重复的超分子结构分析,如多核糖体和全细胞;能够为超分子组织提供前所未有的信息(可视化蛋白质组学)。
关键词:冷冻透射电镜;单颗粒;蛋白复合物
Abstract:
Abstract: Single particle electron microscopy has become a powerful method for studying large protein complexes and, in conjunction with other methods, can provide structural models at (pseudo) atomic resolution. This will be exemplified with two large proteolytic complexes, tripeptidyl peptidase II (6 MDa) and the 26S proteasome (2.5 MDa). Cryo-electron tomography enables the structural analysis of non-repetitive supramolecular structures, such as polyribosomes and even whole cells providing unprecedented insights into their supramolecular organization (visual proteomics).
Key words: cryo-electron microscopy; single particle; protein complexes