title: What can electron microscopy tell us about chaperoned protein folding?
abstract: Chaperonins form large, cage-like structures that act as protein folding machines. Recent developments in electron cryo-microscopy and image processing are helping to reveal the mechanism of chaperonin-mediated protein folding.
authors.affiliation: Department of Crystallography, Birkbeck College London, UK. h.saibil@cryst.bbk.ac.uk
authors.forename: H R
authors.initials: HR
authors.lastname: Saibil
mesh_terms: D000818:Animals; D018835:Chaperonin 10 / Q000737:chemistry / Q000648:ultrastructure; D018834:Chaperonin 60 / Q000737:chemistry / Q000648:ultrastructure; D018833:Chaperonins / Q000737:chemistry* / Q000648:ultrastructure*; D007091:Image Processing, Computer-Assisted / Q000379:methods; D008854:Microscopy, Electron / Q000379:methods*; D017510:Protein Folding; D012996:Solutions
chemical_list: D018835:Chaperonin 10; D018834:Chaperonin 60; D012996:Solutions; D018833:Chaperonins