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Open data
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Basic information
Entry | Database: PDB / ID: 9h7v | ||||||||||||||||||||||||
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Title | The baseplate assembly of Haloferax tailed virus 1. | ||||||||||||||||||||||||
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![]() | VIRUS / Archaeal virus / tail / baseplate / tail fiber | ||||||||||||||||||||||||
Function / homology | : / Baseplate hub / Tail tube protein / Phate tail tape measure protein / Uncharacterized protein / Uncharacterized protein![]() | ||||||||||||||||||||||||
Biological species | ![]() | ||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.6 Å | ||||||||||||||||||||||||
![]() | Zhang, D. / Daum, B. / Isupov, M.N. / McLaren, M. | ||||||||||||||||||||||||
Funding support | European Union, 1items
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![]() | ![]() Title: The baseplate assembly of Haloferax tailed virus 1. Authors: Zhang, D. / Daum, B. / Isupov, M.N. / McLaren, M. / Oksanen, H. / Quax, T.E.F. / Schwarzer, S. / Gold, V.A.M. / Stuart, W. | ||||||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.3 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.4 MB | Display | ![]() |
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Full document | ![]() | 1.4 MB | Display | |
Data in XML | ![]() | 171.2 KB | Display | |
Data in CIF | ![]() | 275.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 51915MC M: map data used to model this data C: citing same article ( |
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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 , 5 types, 27 molecules B1B2B3B4B5B6BABBBCBDBEBFBGBHBIBJBKBLBMBNBOQEQFQGQHQIQJ
#1: Protein | Mass: 17177.463 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Protein | Mass: 30425.914 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 102541.312 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 29020.555 Da / Num. of mol.: 9 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | Mass: 36043.656 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 3 types, 62 molecules 




#6: Chemical | ChemComp-MG / #7: Chemical | ChemComp-K / #8: Chemical | ChemComp-ZN / |
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-Details
Has ligand of interest | Y |
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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: Haloferax tailed virus 1 / Type: VIRUS / Entity ID: #1-#2, #5 / Source: NATURAL |
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Source (natural) | Organism: ![]() |
Details of virus | Empty: NO / Enveloped: NO / Isolate: OTHER / Type: VIRION |
Natural host | Organism: Haloferax gibbonsii |
Buffer solution | pH: 7 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: TFS KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm / Cs: 2.7 mm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k) |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||
3D reconstruction | Resolution: 2.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 135152 / Symmetry type: POINT |