ArticleMethods in molecular biology (Clifton, N.J.)2014
Single particle cryo-electron microscopy and 3-D reconstruction of viruses.
Article in Methods in molecular biology (Clifton, N.J.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.
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96 citing papers in PubMed.
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- STT3A-mediated viral N-glycosylation underlies the tumor selectivity of oncolytic virus M1.Oncogene · 2023Article
- Overview of Membrane Protein Sample Preparation for Single-Particle Cryo-Electron Microscopy Analysis.International journal of molecular sciences · 2023Review
- Development of Single Molecule Techniques for Sensing and Manipulation of CRISPR and Polymerase Enzymes.Small (Weinheim an der Bergstrasse, Germany) · 2023Review
- Structure ofViruses · 2023Article
- The structure of a 12-segmented dsRNA reovirus: New insights into capsid stabilization and organization.PLoS pathogens · 2023Article
- Structural constraints link differences in neutralization potency of human anti-Eastern equine encephalitis virus monoclonal antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- prM-reactive antibodies reveal a role for partially mature virions in dengue virus pathogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The αTSR Domain ofInternational journal of nanomedicine · 2023Article
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- Near-atomic, non-icosahedrally averaged structure of giant virus Paramecium bursaria chlorella virus 1.Nature communications · 2022Article
- Structures of a large prolate virus capsid in unexpanded and expanded states generate insights into the icosahedral virus assembly.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Cryo-EM structures of alphavirus conformational intermediates in low pH-triggered prefusion states.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structure of infective Getah virus at 2.8 Å resolution determined by cryo-electron microscopy.Cell discovery · 2022Article
- Determining structures in a native environment using single-particle cryoelectron microscopy images.Innovation (Cambridge (Mass.)) · 2021Article
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- Structure of Usutu virus SAAR-1776 displays fusion loop asymmetry.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Affinity Capture of p97 with Small-Molecule Ligand Bait Reveals a 3.6 Å Double-Hexamer Cryoelectron Microscopy Structure.ACS nano · 2021Article
- Sizing Extracellular Vesicles Using Membrane Dyes and a Single Molecule-Sensitive Flow Analyzer.Analytical chemistry · 2021Article
36 more citing papers are in PubMed but not listed here.
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2 authors.
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Abstract
With fast progresses in instrumentation, image processing algorithms, and computational resources, single particle electron cryo-microscopy (cryo-EM) 3-D reconstruction of icosahedral viruses has now reached near-atomic resolutions (3-4 Å). With comparable resolutions and more predictable outcomes, cryo-EM is now considered a preferred method over X-ray crystallography for determination of atomic structure of icosahedral viruses. At near-atomic resolutions, all-atom models or backbone models can be reliably built that allow residue level understanding of viral assembly and conformational changes among different stages of viral life cycle. With the developments of asymmetric reconstruction, it is now possible to visualize the complete structure of a complex virus with not only its icosahedral shell but also its multiple non-icosahedral structural features. In this chapter, we will describe single particle cryo-EM experimental and computational procedures for both near-atomic resolution reconstruction of icosahedral viruses and asymmetric reconstruction of viruses with both icosahedral and non-icosahedral structure components. Procedures for rigorous validation of the reconstructions and resolution evaluations using truly independent de novo initial models and refinements are also introduced.
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