Supplanting crystallography or supplementing microscopy? A combined approach to the study of an enveloped virus.
The recent advances in the resolution obtained by single-particle reconstructions from cryo-electron microscopy (cryo-EM) have led to an increase in studies that combine X-ray crystallographic results with those of electron microscopy (EM). Here, such a combination is described in the determination of the structure of an enveloped animal virus, Semliki Forest virus, at 9 A resolution. The issues of model bias in determination of the structure, the definition of resolution in a single-particle reconstruction, the effect of the correction of the contrast-transfer function on the structure determined and the use of a high-resolution structure of a subunit in the interpretation of the structure of the complex are addressed.
Mancini
E J
EJ
The Structural Biology Programme, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
Fuller
S D
SD
D000818:Animals; D001436:Bacteriorhodopsins / Q000737:chemistry / Q000648:ultrastructure; D020285:Cryoelectron Microscopy / Q000379:methods; D018360:Crystallography, X-Ray / Q000379:methods; D007091:Image Processing, Computer-Assisted / Q000379:methods*; D008958:Models, Molecular; D008961:Models, Structural; D019251:Nucleocapsid / Q000737:chemistry* / Q000648:ultrastructure*; D011487:Protein Conformation; D015203:Reproducibility of Results; D012270:Ribosomes / Q000648:ultrastructure; D012672:Semliki forest virus / Q000648:ultrastructure*; D014404:Tubulin / Q000737:chemistry / Q000648:ultrastructure
D014404:Tubulin; D001436:Bacteriorhodopsins