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- PDB-9qzf: Proximal A-C linker of Tetrahymena centriole, six repeating units -
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Open data
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Basic information
Entry | Database: PDB / ID: 9qzf | |||||||||||||||
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Title | Proximal A-C linker of Tetrahymena centriole, six repeating units | |||||||||||||||
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![]() | STRUCTURAL PROTEIN / centriole / basal body / centrosome | |||||||||||||||
Function / homology | ![]() MWP complex / cell projection organization / centrosome cycle / microtubule organizing center / cilium assembly / centriole / centriolar satellite / ciliary basal body / centrosome / cytoplasm Similarity search - Function | |||||||||||||||
Biological species | ![]() ![]() | |||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.8 Å | |||||||||||||||
![]() | Cai, B. / Xu, J.W. / Luo, L. / Aarts, E. / Leitner, A. / Ishikawa, T. / Beltro, P. / Pilhofer, M. / Wieczorek, M. | |||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure and assembly of the A-C linker connecting microtubule triplets in centrioles Authors: Cai, B. / Xu, J.W. / Luo, L. / Aarts, E. / Leitner, A. / Ishikawa, T. / Beltro, P. / Pilhofer, M. / Wieczorek, M. | |||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 3.6 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 688.1 KB | Display | ![]() |
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Full document | ![]() | 687.3 KB | Display | |
Data in XML | ![]() | 279.3 KB | Display | |
Data in CIF | ![]() | 432.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 53471MC ![]() 9qzcC 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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Components
-Protein , 6 types, 54 molecules ACiBDCPCaDfkqsyBKBRCWCdChzEIn17BYGLMRv9...
#1: Protein | Mass: 51977.465 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Protein | Mass: 44594.297 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #3: Protein | Mass: 110098.609 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #5: Protein | Mass: 141643.859 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #7: Protein | Mass: 71408.133 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #16: Protein | Mass: 26274.373 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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-Unknown Protein ... , 10 types, 60 molecules FdoBOBZBwHlwBVBgB4Kt5BcBnCAN2ACBjBuCHPUAJAWAcB1...
#4: Protein | Mass: 12868.854 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #6: Protein | Mass: 13975.214 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #8: Protein | Mass: 14230.525 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #9: Protein | Mass: 13719.902 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #10: Protein/peptide | Mass: 2741.370 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #11: Protein | Mass: 8954.028 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #12: Protein/peptide | Mass: 2826.475 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #13: Protein | Mass: 10826.337 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #14: Protein | Mass: 13039.064 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #15: Protein | Mass: 8698.714 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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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: FILAMENT / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: proximal A-C linker of Tetrahymena thermophila basal body centriole Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: #1-#2, #4, #6-#16, #3, #5 / Source: NATURAL |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE-PROPANE |
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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: 3000 nm / Nominal defocus min: 800 nm |
Image recording | Electron dose: 35 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||
3D reconstruction | Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 155485 / Symmetry type: POINT |