Supplanting crystallography or supplementing microscopy? A combined approach to the study of an enveloped virus

Acta Crystallogr D Biol Crystallogr. 2000 Oct;56(Pt 10):1278-87. doi: 10.1107/s0907444900010817.

Abstract

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.

MeSH terms

  • Animals
  • Bacteriorhodopsins / chemistry
  • Bacteriorhodopsins / ultrastructure
  • Cryoelectron Microscopy / methods
  • Crystallography, X-Ray / methods
  • Image Processing, Computer-Assisted / methods*
  • Models, Molecular
  • Models, Structural
  • Nucleocapsid / chemistry*
  • Nucleocapsid / ultrastructure*
  • Protein Conformation*
  • Reproducibility of Results
  • Ribosomes / ultrastructure
  • Semliki forest virus / ultrastructure*
  • Tubulin / chemistry
  • Tubulin / ultrastructure

Substances

  • Tubulin
  • Bacteriorhodopsins