Electron cryomicroscopy methods.
Electron cryomicroscopy methods comprise a rapidly expanding field providing insights into the structure and function of biological macromolecules and their supramolecular assemblies. The 3.8 A resolution structure of the membrane protein aquaporin, a view of the herpesvirus capsid at 8.5 A and the 10 A resolution structure of the spliceosomal U1 small nuclear ribonucleoprotein complex are three outstanding examples emphasizing the versatility of this technique.
Unger
V M
VM
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8024, USA. vinzenz.unger@yale.edu
D020346:Aquaporins / Q000737:chemistry / Q000648:ultrastructure; D002213:Capsid / Q000737:chemistry / Q000648:ultrastructure; D020285:Cryoelectron Microscopy / Q000379:methods*; D003461:Crystallography / Q000379:methods; D006564:Herpesviridae / Q000737:chemistry / Q000648:ultrastructure; D007091:Image Processing, Computer-Assisted; D046911:Macromolecular Substances; D008958:Models, Molecular; D011487:Protein Conformation; D017412:Ribonucleoprotein, U1 Small Nuclear / Q000737:chemistry / Q000648:ultrastructure; D012995:Solubility; D014054:Tomography / Q000379:methods
D020346:Aquaporins; D046911:Macromolecular Substances; D017412:Ribonucleoprotein, U1 Small Nuclear