+Open data
-Basic information
Entry | Database: PDB / ID: 7wmp | |||||||||
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Title | Tail structure of Helicobacter pylori bacteriophage KHP30 | |||||||||
Components |
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Keywords | VIRAL PROTEIN / PHAGE / PHAGE TAIL / CRYOEM / VIRUS | |||||||||
Function / homology | symbiont genome ejection through host cell envelope, short tail mechanism / viral capsid / Uncharacterized protein / Phage protein / Portal protein Function and homology information | |||||||||
Biological species | Helicobacter phage KHP30 (virus) | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||
Authors | Kamiya, R. / Uchiyama, J. / Matsuzaki, S. / Murata, K. / Iwasaki, K. / Miyazaki, N. | |||||||||
Funding support | Japan, 2items
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Citation | Journal: To Be Published Title: Cryo-EM structure of Helicobacter pylori bacteriophage KHP30 Authors: Kamiya, R. / Uchiyama, J. / Matsuzaki, S. / Murata, K. / Iwasaki, K. / Miyazaki, N. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7wmp.cif.gz | 2 MB | Display | PDBx/mmCIF format |
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PDB format | pdb7wmp.ent.gz | 1.7 MB | Display | PDB format |
PDBx/mmJSON format | 7wmp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7wmp_validation.pdf.gz | 885.2 KB | Display | wwPDB validaton report |
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Full document | 7wmp_full_validation.pdf.gz | 920.5 KB | Display | |
Data in XML | 7wmp_validation.xml.gz | 267.9 KB | Display | |
Data in CIF | 7wmp_validation.cif.gz | 399.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wm/7wmp ftp://data.pdbj.org/pub/pdb/validation_reports/wm/7wmp | HTTPS FTP |
-Related structure data
Related structure data | 32616MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 69634.734 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Helicobacter phage KHP30 (virus) / References: UniProt: I7HHN4 #2: Protein | Mass: 22609.309 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Helicobacter phage KHP30 (virus) / References: UniProt: I7HHN3 #3: Protein | Mass: 29741.775 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Helicobacter phage KHP30 (virus) / References: UniProt: I7HFX1 |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Helicobacter phage KHP / Type: VIRUS / Entity ID: all / Source: NATURAL |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: Helicobacter phage KHP (virus) |
Details of virus | Empty: NO / Enveloped: NO / Isolate: OTHER / Type: VIRION |
Virus shell | Name: Head / Diameter: 700 nm / Triangulation number (T number): 9 |
Buffer solution | pH: 7.2 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
-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: 1000 nm / Cs: 2.7 mm |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Average exposure time: 2.5 sec. / Electron dose: 50 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON III (4k x 4k) |
-Processing
EM software | Name: RELION / Version: 3 / Category: 3D reconstruction |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
Particle selection | Num. of particles selected: 32655 |
Symmetry | Point symmetry: C12 (12 fold cyclic) |
3D reconstruction | Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 27422 / Symmetry type: POINT |