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TitleCryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki Forest virus.
Journal, issue, pagesMol Cell, Vol. 5, Issue 2, Page 255-266, Year 2000
Publish dateJul 17, 2000
AuthorsE J Mancini / M Clarke / B E Gowen / T Rutten / S D Fuller /
PubMed AbstractSemliki Forest virus serves as a paradigm for membrane fusion and assembly. Our icosahedral reconstruction combined 5276 particle images from 48 cryo-electron micrographs and determined the virion ...Semliki Forest virus serves as a paradigm for membrane fusion and assembly. Our icosahedral reconstruction combined 5276 particle images from 48 cryo-electron micrographs and determined the virion structure to 9 A resolution. The improved resolution of this map reveals an N-terminal arm linking capsid subunits and defines the spike-capsid interaction sites. It illustrates the paired helical nature of the transmembrane segments and the elongated structures connecting them to the spike projecting domains. A 10 A diameter density in the fusion protein lines the cavity at the center of the spike. These clearly visible features combine with the variation in order between the layers to provide a framework for understanding the structural changes during the life cycle of an enveloped virus.
External linksMol Cell / PubMed:10882067
MethodsEM (single particle)
Resolution9.0 Å
Structure data

1015

1dyl

EMDB-1015: Cryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki Forest virus.
PDB-1dyl: 9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY
Method: EM (single particle) / Resolution: 9.0 Å

Source
  • semliki forest virus
KeywordsVIRUS/VIRAL PROTEIN / ALPHAVIRUS / SFV / CRYO-EM / IMAGE RECONSTRUCTION / ENVELOPED VIRUS / CAPSID PROTEIN / ICOSAHEDRAL VIRUS / VIRUS-VIRAL PROTEIN complex

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