Department of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, D-60438 Frankfurt am Main, Germany.
Department of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, D-60438 Frankfurt am Main, Germany.
Curr Opin Struct Biol. 2017 Oct;46:48-54. doi: 10.1016/j.sbi.2017.05.016. Epub 2017 Jul 17.
Recent advances in cryo-electron microscopy instrumentation and software have made it possible to obtain atomic resolution structures of macromolecular complexes with a small amount of material at low concentration and without the need for crystallisation. Oligomeric enzymes are particularly well suited for this technique because of their symmetry and often large size or rigid structure and can be used to explore the limits of the technique. Conformational changes can reach their full extent in solution, not hampered by crystal contacts, and multiple conformations in a sample can be separated computationally. Cryo-EM structures can be solved de novo for large complexes that resist crystallisation or structure determination by crystallographic techniques.
近年来，低温电子显微镜仪器和软件的发展使得人们有可能在低浓度、无需结晶的情况下，用少量材料获得大分子复合物的原子分辨率结构。寡聚酶特别适合这种技术，因为它们具有对称性，而且通常体积较大或结构较硬，可以用来探索该技术的极限。构象变化可以在溶液中充分展开，不受晶体接触的阻碍，并且可以通过计算将样品中的多个构象分开。对于那些难以结晶或通过晶体学技术确定结构的大复合物，可以通过从头开始解决低温电子显微镜结构问题。
