Cargando…
High-resolution cryo-EM structures of outbreak strain human norovirus shells reveal size variations
Noroviruses are a leading cause of foodborne illnesses worldwide. Although GII.4 strains have been responsible for most norovirus outbreaks, the assembled virus shell structures have been available in detail for only a single strain (GI.1). We present high-resolution (2.6- to 4.1-Å) cryoelectron mic...
Autores principales: | Jung, James, Grant, Timothy, Thomas, Dennis R., Diehnelt, Chris W., Grigorieff, Nikolaus, Joshua-Tor, Leemor |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
National Academy of Sciences
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6601263/ https://www.ncbi.nlm.nih.gov/pubmed/31182604 http://dx.doi.org/10.1073/pnas.1903562116 |
Ejemplares similares
-
The dynamic nature of the human origin recognition complex revealed through five cryoEM structures
por: Jaremko, Matt J, et al.
Publicado: (2020) -
Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6
por: Grant, Timothy, et al.
Publicado: (2015) -
Dynamics in the murine norovirus capsid revealed by high-resolution cryo-EM
por: Snowden, Joseph S., et al.
Publicado: (2020) -
Ensemble cryo-EM elucidates the mechanism of translation fidelity
por: Loveland, Anna B., et al.
Publicado: (2017) -
Single-protein detection in crowded molecular environments in cryo-EM images
por: Rickgauer, J Peter, et al.
Publicado: (2017)