+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-4462 | ||||||||||||
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Title | Vertex Complex of Bacteriophage PR772 | ||||||||||||
Map data | |||||||||||||
Sample |
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Biological species | Enterobacteria phage PR772 (virus) | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 10.0 Å | ||||||||||||
Authors | Narayana Reddy HK / Svenda M | ||||||||||||
Funding support | Sweden, 3 items
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Citation | Journal: Elife / Year: 2019 Title: Electron cryo-microscopy of bacteriophage PR772 reveals the elusive vertex complex and the capsid architecture. Authors: Hemanth Kn Reddy / Marta Carroni / Janos Hajdu / Martin Svenda / Abstract: Bacteriophage PR772, a member of the family, has a 70 nm diameter icosahedral protein capsid that encapsulates a lipid membrane, dsDNA, and various internal proteins. An icosahedrally averaged ...Bacteriophage PR772, a member of the family, has a 70 nm diameter icosahedral protein capsid that encapsulates a lipid membrane, dsDNA, and various internal proteins. An icosahedrally averaged CryoEM reconstruction of the wild-type virion and a localized reconstruction of the vertex region reveal the composition and the structure of the vertex complex along with new protein conformations that play a vital role in maintaining the capsid architecture of the virion. The overall resolution of the virion is 2.75 Å, while the resolution of the protein capsid is 2.3 Å. The conventional penta-symmetron formed by the capsomeres is replaced by a large vertex complex in the pseudo T = 25 capsid. All the vertices contain the host-recognition protein, P5; two of these vertices show the presence of the receptor-binding protein, P2. The 3D structure of the vertex complex shows interactions with the viral membrane, indicating a possible mechanism for viral infection. | ||||||||||||
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_4462.map.gz | 9 MB | EMDB map data format | |
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Header (meta data) | emd-4462-v30.xml emd-4462.xml | 9.9 KB 9.9 KB | Display Display | EMDB header |
Images | emd_4462.png | 32.2 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-4462 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-4462 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_4462.map.gz / Format: CCP4 / Size: 10.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Voxel size | X=Y=Z: 2.12 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 PR772
Entire | Name: Enterobacteria phage PR772 (virus) |
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Components |
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-Supramolecule #1: Enterobacteria phage PR772
Supramolecule | Name: Enterobacteria phage PR772 / type: virus / ID: 1 / Parent: 0 / NCBI-ID: 261665 / Sci species name: Enterobacteria phage PR772 / Virus type: VIRION / Virus isolate: SEROTYPE / Virus enveloped: No / Virus empty: No |
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Host (natural) | Organism: Escherichia coli (E. coli) / Strain: K12 J53-1(R15) [HER 1221] |
Molecular weight | Theoretical: 500 KDa |
Virus shell | Shell ID: 1 / Diameter: 700.0 Å / T number (triangulation number): 25 |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 7 mg/mL |
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Buffer | pH: 8 Details: HEPES 20 mM, NaCl 100 mM, MgSO4 1 mM, EDTA 1 mM, pH 8.0 |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 298 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 2.6 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 130000 |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: INTEGRATING / Number real images: 3200 / Average exposure time: 9.0 sec. / Average electron dose: 4.4 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Particle selection | Number selected: 256000 / Details: Total sub-particles extracted. |
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Initial angle assignment | Type: NOT APPLICABLE |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |
Final reconstruction | Number classes used: 6 / Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 10.0 Å / Resolution method: OTHER / Details: Localized Reconstruction / Number images used: 41000 |
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: OTHER |
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