Envelope structure of Semliki Forest virus reconstructed from cryo-electron micrographs

Détails

ID Serval
serval:BIB_2A91AAA28320
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Envelope structure of Semliki Forest virus reconstructed from cryo-electron micrographs
Périodique
Nature
Auteur(s)
Vogel  R. H., Provencher  S. W., von Bonsdorff  C. H., Adrian  M., Dubochet  J.
ISSN
0028-0836 (Print)
Statut éditorial
Publié
Date de publication
04/1986
Volume
320
Numéro
6062
Pages
533-5
Notes
Journal Article --- Old month value: Apr 10-16
Résumé
The basic principles of the architecture of many viral protein shells have been successfully established from electron microscopy and X-ray data, but enveloped viruses have been more difficult to study because they resist crystallization and are easily deformed when prepared for electron microscopy. To avoid the limitations of conventional techniques when applied to enveloped viruses, we have used a cryo-electron microscopy method in which unfixed and unstained viruses are observed in an unsupported thin layer of vitrified suspension. Because of electron beam damage, the many different views required for high-resolution three-dimensional reconstruction cannot be obtained from a tilt series of the same particle. The images of many differently oriented viruses are combined using a novel reconstruction method, 'reconstruction by optimized series expansion' (ROSE). The structure of the envelope of Semliki Forest virus has been reconstructed to 3.5-nm resolution. The T = 4 geometry of the surface lattice, the shape of the trimeric spikes and their arrangement on the lipid bilayer are visualized.
Mots-clé
Freezing Membrane Lipids/analysis Microscopy, Electron Models, Structural Semliki forest virus/*ultrastructure Viral Envelope Proteins/*analysis
Pubmed
Web of science
Création de la notice
24/01/2008 10:25
Dernière modification de la notice
20/08/2019 13:10
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