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Open data
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Basic information
| Entry | Database: PDB / ID: 8xan | |||||||||
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| Title | Major tail protein of SH-Ab15497 | |||||||||
Components | Major tail structural protein | |||||||||
Keywords | VIRAL PROTEIN / helical reconstruction / C3 symmetry | |||||||||
| Function / homology | Phage tail tube protein-like / Phage tail tube protein / Major tail structural protein Function and homology information | |||||||||
| Biological species | Acinetobacter phage SH-Ab 15497 (virus) | |||||||||
| Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
Authors | Lin, J. / Zhao, S.W. | |||||||||
| Funding support | China, 2items
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Citation | Journal: To Be PublishedTitle: Major tail protein of SH-Ab15497 Authors: Lin, J. / Zhao, S.W. | |||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8xan.cif.gz | 176.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8xan.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8xan.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8xan_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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| Full document | 8xan_full_validation.pdf.gz | 1.3 MB | Display | |
| Data in XML | 8xan_validation.xml.gz | 37.4 KB | Display | |
| Data in CIF | 8xan_validation.cif.gz | 55.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xa/8xan ftp://data.pdbj.org/pub/pdb/validation_reports/xa/8xan | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 38202MC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 33208.465 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Acinetobacter phage SH-Ab 15497 (virus) / References: UniProt: A0A2H5BHH8Has protein modification | N | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: helical reconstruction |
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Sample preparation
| Component | Name: Acinetobacter phage SH-Ab 15497 / Type: VIRUS / Entity ID: all / Source: NATURAL | ||||||||||||||||||||
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| Source (natural) | Organism: Acinetobacter phage SH-Ab 15497 (virus) | ||||||||||||||||||||
| Details of virus | Empty: NO / Enveloped: NO / Isolate: OTHER / Type: VIRION | ||||||||||||||||||||
| Virus shell | Diameter: 650 nm / Triangulation number (T number): 7 | ||||||||||||||||||||
| Buffer solution | pH: 7.5 | ||||||||||||||||||||
| Buffer component |
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| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / 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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1200 nm / Cs: 2.7 mm |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of real images: 27057 |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| Helical symmerty | Angular rotation/subunit: 40.7 ° / Axial rise/subunit: 38.3 Å / Axial symmetry: C3 | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 157605 / Symmetry type: HELICAL | ||||||||||||||||||||||||
| Atomic model building | Source name: AlphaFold / Type: in silico model | ||||||||||||||||||||||||
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About Yorodumi




Acinetobacter phage SH-Ab 15497 (virus)
China, 2items
Citation
PDBj

FIELD EMISSION GUN