Conformational changes studied by cryo-electron microscopy.
Biological processes involving movement, such as muscle contraction or the opening of an ion channel through a membrane, are mediated through conformational changes. These changes often occur in large and flexible macromolecular complexes. Cryo-electron microscopy provides a means of capturing different conformational states of such assemblies. Even if the resulting density maps are at low resolution, they can be combined with atomic structures of subcomplexes or isolated components determined by X-ray crystallography or NMR. This review presents a brief summary of the principles and recent advances in macromolecular structure determination by cryo-electron microscopy.
Saibil
H R
HR
Crystallography Department, Birkbeck College, Malet Street, London WC1E 7HX, UK. h.saibil@mail.cryst.bbk.ac.uk
D000818:Animals; D001426:Bacterial Proteins; D018833:Chaperonins / Q000737:chemistry / Q000378:metabolism; D020285:Cryoelectron Microscopy / Q000295:instrumentation / Q000379:methods*; D006801:Humans; D007091:Image Processing, Computer-Assisted; D007700:Kinetics; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D011978:Receptors, Nicotinic / Q000737:chemistry / Q000378:metabolism; D012270:Ribosomes / Q000737:chemistry / Q000378:metabolism; D012672:Semliki forest virus / Q000737:chemistry / Q000502:physiology; D013301:Streptolysins / Q000737:chemistry / Q000378:metabolism
D001426:Bacterial Proteins; D020409:Molecular Motor Proteins; D011506:Proteins; D011978:Receptors, Nicotinic; D013301:Streptolysins; C032290:plY protein, Streptococcus pneumoniae; D018833:Chaperonins