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- PDB-9euf: Cryo-EM structure of Staphylococcus aureus bacteriophage phi812 b... -
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Open data
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Basic information
Entry | Database: PDB / ID: 9euf | |||||||||||||||||||||||||||
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Title | Cryo-EM structure of Staphylococcus aureus bacteriophage phi812 baseplate in the pre-contraction state - complete | |||||||||||||||||||||||||||
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![]() | VIRUS / bacteriophage / phage / contractile / phi812 / baseplate | |||||||||||||||||||||||||||
Function / homology | ![]() symbiont-mediated cytolysis of host cell / hydrolase activity, acting on glycosyl bonds / phosphoric diester hydrolase activity / cysteine-type peptidase activity / lipid metabolic process Similarity search - Function | |||||||||||||||||||||||||||
Biological species | ![]() | |||||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 7.3 Å | |||||||||||||||||||||||||||
![]() | Binovsky, J. / Siborova, M. / Baska, R. / Pichel-Beleiro, A. / Skubnik, K. / Novacek, J. / Benesik, M. / van Raaij, M.J. / Plevka, P. | |||||||||||||||||||||||||||
Funding support | European Union, ![]()
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![]() | ![]() Title: Cell attachment and tail contraction of S. aureus phage phi812 Authors: Binovsky, J. / Siborova, M. / Baska, R. / Pichel-Beleiro, A. / Skubnik, K. / Novacek, J. / Benesik, M. / van Raaij, M.J. / 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 | ![]() | 5.4 MB | 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 | ![]() 19968MC ![]() 9eugC ![]() 9euhC ![]() 9euiC ![]() 9eujC ![]() 9eukC ![]() 9eulC ![]() 9eumC ![]() 9f04C ![]() 9f05C ![]() 9f06C ![]() 9fkoC 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 , 14 types, 63 molecules 01234hijklmz567nop89AAqrsABCDIK...
#1: Protein | Mass: 129262.961 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Protein | Mass: 50474.078 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 72654.742 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | | Mass: 34645.887 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | | Mass: 96199.547 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | Mass: 39248.859 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein | | Mass: 91364.289 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | Mass: 19998.748 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | Mass: 116389.945 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | Mass: 26611.752 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein | Mass: 29381.604 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | Mass: 64559.008 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #13: Protein | Mass: 15942.970 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #14: Protein | Mass: 21588.104 Da / Num. of mol.: 12 Source method: isolated from a genetically manipulated source Details: recombinantly expressed structure; protein-linker-His6tag; linker+His6tag: DPNSSSVDKLAAALEHHHHHH Source: (gene. exp.) ![]() Gene: 812_119, 812_121, 812a_121, 812F1_121, K1/420_121, K1_121 Production host: ![]() ![]() |
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-Details
Has 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: single particle reconstruction |
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Sample preparation
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Source (natural) |
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Source (recombinant) | Organism: ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||
Details of virus | Empty: NO / Enveloped: NO / Isolate: SPECIES / Type: VIRION | ||||||||||||||||||||||||||||||||||||||||||||||||
Natural host | Organism: SA 812 | ||||||||||||||||||||||||||||||||||||||||||||||||
Buffer solution | pH: 8 / Details: 50mM Tris, 10mM NaCl, 10mM CaCl2 | ||||||||||||||||||||||||||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||||||||||||||||||||
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 / Humidity: 100 % / Chamber temperature: 277 K |
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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: 3000 nm / Nominal defocus min: 800 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm |
Image recording | Average exposure time: 1 sec. / Electron dose: 48 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON II (4k x 4k) |
Image scans | Movie frames/image: 18 |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 23421 | ||||||||||||||||||||||||||||
Symmetry | Point symmetry: C3 (3 fold cyclic) | ||||||||||||||||||||||||||||
3D reconstruction | Resolution: 7.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 9705 / Symmetry type: POINT | ||||||||||||||||||||||||||||
Atomic model building | Protocol: RIGID BODY FIT / Space: REAL |