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Open data
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Basic information
Entry | Database: PDB / ID: 8r69 | ||||||
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Title | Neck and tail of phage 812 virion (composite) | ||||||
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![]() | VIRUS / phage / neck / connector / tail | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.3 Å | ||||||
![]() | Cienikova, Z. / Novacek, J. / Fuzik, T. / Benesik, M. / Plevka, P. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Genome anchoring, retention, and release by neck proteins of Herelleviridae phage 812 Authors: Cienikova, Z. / Novacek, J. / Siborova, M. / Popelarova, B. / Fuzik, T. / Benesik, M. / Bardy, P. / Pantucek, R. / Plevka, P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 669.5 KB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 18949MC ![]() 8q01C ![]() 8q1iC ![]() 8q7dC ![]() 8qekC ![]() 8qemC ![]() 8qgrC ![]() 8qjeC ![]() 8qkhC ![]() 8r5gC C: citing same article ( M: map data used to model this data |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Components
-Protein , 8 types, 14 molecules TUVWABEGNnSsCD
#1: Protein | Mass: 15942.970 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Protein | Mass: 64559.008 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 64155.684 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | | Mass: 33757.332 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | | Mass: 31799.680 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | Mass: 10146.707 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein | Mass: 17885.197 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | Mass: 34191.703 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 1 types, 3 molecules 
#9: Chemical |
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-Details
Has ligand of interest | N |
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Has protein modification | N |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: Staphylococcus phage 812 / Type: VIRUS / Details: Purified phage virion / Entity ID: #1-#8 / Source: NATURAL | ||||||||||||||||||||
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Molecular weight | Experimental value: NO | ||||||||||||||||||||
Source (natural) | Organism: ![]() | ||||||||||||||||||||
Details of virus | Empty: NO / Enveloped: NO / Isolate: SPECIES / Type: VIRION | ||||||||||||||||||||
Natural host | Organism: Staphylococcus aureus / Strain: CCM 8428 | ||||||||||||||||||||
Virus shell | Diameter: 1100 nm | ||||||||||||||||||||
Buffer solution | pH: 8 | ||||||||||||||||||||
Buffer component |
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Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: Purified virion particles | ||||||||||||||||||||
Specimen support | Grid material: COPPER / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R2/1 | ||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE-PROPANE / Humidity: 100 % |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 75000 X / Nominal defocus max: 2400 nm / Nominal defocus min: 1200 nm / Cs: 2.7 mm |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Average exposure time: 1 sec. / Electron dose: 49 e/Å2 / Film or detector model: FEI FALCON II (4k x 4k) / Num. of real images: 30553 |
Image scans | Width: 4000 / Height: 4000 / Movie frames/image: 16 |
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Processing
EM software |
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Image processing | Details: Frame alignment and dose-weighting with motioncor2, then contrast inversion and normalization | ||||||||||||||||||||||||||||||||||||
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 23947 / Details: Manual particle selection | ||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: C6 (6 fold cyclic) | ||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 4.3 Å / Resolution method: OTHER / Num. of particles: 21731 / Algorithm: FOURIER SPACE Details: This is a composite map created by merging two focused reconstructions. The composite map was then low-pass filtered to the (gold-standard cut-off 0.143) resolution of the input ...Details: This is a composite map created by merging two focused reconstructions. The composite map was then low-pass filtered to the (gold-standard cut-off 0.143) resolution of the input reconstruction with worse resolution. Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: RIGID BODY FIT / Target criteria: cross-correlation coefficient | ||||||||||||||||||||||||||||||||||||
Atomic model building |
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