+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-7315 | |||||||||
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Title | Bacteriophage P22 gp26minus symmetric reconstruction | |||||||||
Map data | Bacteriophage P22 gp26 minus icosahedral reconstruction | |||||||||
Sample |
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Biological species | Enterobacteria phage P22 (virus) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 7.8 Å | |||||||||
Authors | McNulty R / Johnson JE | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Biophys J / Year: 2018 Title: Cryo-EM Elucidation of the Structure of Bacteriophage P22 Virions after Genome Release. Authors: Reginald McNulty / Giovanni Cardone / Eddie B Gilcrease / Timothy S Baker / Sherwood R Casjens / John E Johnson / Abstract: Genome ejection proteins are required to facilitate transport of bacteriophage P22 double-stranded DNA safely through membranes of Salmonella. The structures and locations of all proteins in the ...Genome ejection proteins are required to facilitate transport of bacteriophage P22 double-stranded DNA safely through membranes of Salmonella. The structures and locations of all proteins in the context of the mature virion are known, with the exception of three ejection proteins. Furthermore, the changes that occur to the proteins residing in the mature virion upon DNA release are not fully understood. We used cryogenic electron microscopy to obtain what is, to our knowledge, the first asymmetric reconstruction of mature bacteriophage P22 after double-stranded DNA has been extruded from the capsid-a state representative of one step during viral infection. Results of icosahedral and asymmetric reconstructions at estimated resolutions of 7.8 and 12.5 Å resolutions, respectively, are presented. The reconstruction shows tube-like protein density extending from the center of the tail assembly. The portal protein does not revert to the more contracted, procapsid state, but instead maintains an extended and splayed barrel structure. These structural details contribute to our understanding of the molecular mechanism of P22 phage infection and also set the foundation for future exploitation serving engineering purposes. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_7315.map.gz | 1.2 GB | EMDB map data format | |
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Header (meta data) | emd-7315-v30.xml emd-7315.xml | 8.8 KB 8.8 KB | Display Display | EMDB header |
Images | emd_7315.png | 267.2 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-7315 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-7315 | HTTPS FTP |
-Validation report
Summary document | emd_7315_validation.pdf.gz | 77.5 KB | Display | EMDB validaton report |
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Full document | emd_7315_full_validation.pdf.gz | 76.6 KB | Display | |
Data in XML | emd_7315_validation.xml.gz | 494 B | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-7315 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-7315 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_7315.map.gz / Format: CCP4 / Size: 1.9 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Bacteriophage P22 gp26 minus icosahedral reconstruction | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.58 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : Enterobacteria phage P22
Entire | Name: Enterobacteria phage P22 (virus) |
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Components |
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-Supramolecule #1: Enterobacteria phage P22
Supramolecule | Name: Enterobacteria phage P22 / type: virus / ID: 1 / Parent: 0 / NCBI-ID: 10754 / Sci species name: Enterobacteria phage P22 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: Yes |
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Host system | Organism: Salmonella enterica (bacteria) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Detector mode: COUNTING / Average electron dose: 57.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Talos Arctica / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: PDB ENTRY PDB model - PDB ID: Details: low pass-filtered to 50 angstroms |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 7.8 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: FREALIGN (ver. 9.11) / Number images used: 1935 |
Initial angle assignment | Type: RANDOM ASSIGNMENT / Software - Name: FREALIGN (ver. 9.11) |
Final angle assignment | Type: ANGULAR RECONSTITUTION / Software - Name: FREALIGN (ver. 9.11) |