ArticleProceedings of the National Academy of Sciences of the United States of America2013
Validated near-atomic resolution structure of bacteriophage epsilon15 derived from cryo-EM and modeling.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
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Who cites it
47 citing papers in PubMed, 75 citations in OpenAlex.
- Expanding structural insights into DNA packaging apparatus and endolysin LysSA05 function of Epsilon15 bacteriophage.Frontiers in cellular and infection microbiology · 2025Article
- The structure of a 12-segmented dsRNA reovirus: New insights into capsid stabilization and organization.PLoS pathogens · 2023Article
- A structural dendrogram of the actinobacteriophage major capsid proteins provides important structural insights into the evolution of capsid stability.Structure (London, England : 1993) · 2023Article
- A Capsid Structure ofViruses · 2022Article
- AlphaFold2 and CryoEM: Revisiting CryoEM modeling in near-atomic resolution density maps.iScience · 2022Article
- Predicting the capsid architecture of phages from metagenomic data.Computational and structural biotechnology journal · 2022Article
- Capsid Structure ofJournal of virology · 2021Article
- High Resolution Structure of the Mature Capsid ofInternational journal of molecular sciences · 2021Article
- UCSF ChimeraX: Structure visualization for researchers, educators, and developers.Protein science : a publication of the Protein Society · 2021Article
- The Missing Tailed Phages: Prediction of Small Capsid Candidates.Microorganisms · 2020Article
- Structures of Three Actinobacteriophage Capsids: Roles of Symmetry and Accessory Proteins.Viruses · 2020Article
- Structure and genome ejection mechanism ofScience advances · 2019Article
- The amazing HK97 fold: versatile results of modest differences.Current opinion in virology · 2019Review
- Real-space refinement in PHENIX for cryo-EM and crystallography.Acta crystallographica. Section D, Structural biology · 2018Article
- UCSF ChimeraX: Meeting modern challenges in visualization and analysis.Protein science : a publication of the Protein Society · 2018Article
- Flexible Connectors between Capsomer Subunits that Regulate Capsid Assembly.Journal of molecular biology · 2017Article
- Flexible Fitting of Atomic Models into Cryo-EM Density Maps Guided by Helix Correspondences.Biophysical journal · 2017Article
- CryoEM Structure Refinement by Integrating NMR Chemical Shifts with Molecular Dynamics Simulations.The journal of physical chemistry. B · 2017Article
- Accurate model annotation of a near-atomic resolution cryo-EM map.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Visualizing Adsorption of Cyanophage P-SSP7 onto Marine Prochlorococcus.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
Abstract
High-resolution structures of viruses have made important contributions to modern structural biology. Bacteriophages, the most diverse and abundant organisms on earth, replicate and infect all bacteria and archaea, making them excellent potential alternatives to antibiotics and therapies for multidrug-resistant bacteria. Here, we improved upon our previous electron cryomicroscopy structure of Salmonella bacteriophage epsilon15, achieving a resolution sufficient to determine the tertiary structures of both gp7 and gp10 protein subunits that form the T = 7 icosahedral lattice. This study utilizes recently established best practice for near-atomic to high-resolution (3-5 Å) electron cryomicroscopy data evaluation. The resolution and reliability of the density map were cross-validated by multiple reconstructions from truly independent data sets, whereas the models of the individual protein subunits were validated adopting the best practices from X-ray crystallography. Some sidechain densities are clearly resolved and show the subunit-subunit interactions within and across the capsomeres that are required to stabilize the virus. The presence of the canonical phage and jellyroll viral protein folds, gp7 and gp10, respectively, in the same virus suggests that epsilon15 may have emerged more recently relative to other bacteriophages.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.