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Open data
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Basic information
| Entry | Database: PDB / ID: 9tvu | |||||||||||||||
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| Title | Structure of the Chlamydomonas reinhardtii chlororibosome | |||||||||||||||
Components |
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Keywords | RIBOSOME / chloroplast / translation / chlororibosome | |||||||||||||||
| Function / homology | Function and homology informationmitochondrial large ribosomal subunit / mitochondrial small ribosomal subunit / mitochondrial translation / plastid / chloroplast / large ribosomal subunit / transferase activity / ribosomal small subunit biogenesis / ribosomal large subunit assembly / 5S rRNA binding ...mitochondrial large ribosomal subunit / mitochondrial small ribosomal subunit / mitochondrial translation / plastid / chloroplast / large ribosomal subunit / transferase activity / ribosomal small subunit biogenesis / ribosomal large subunit assembly / 5S rRNA binding / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / response to antibiotic / mRNA binding / mitochondrion / RNA binding / cytoplasm Similarity search - Function | |||||||||||||||
| Biological species | ![]() | |||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.52 Å | |||||||||||||||
Authors | Waltz, F. / Kater, L. / Engel, B.D. | |||||||||||||||
| Funding support | Switzerland, 2items
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Citation | Journal: Biorxiv / Year: 2026Title: Chloroplast-encoded small subunit extensions reshape the Chlamydomonas chlororibosome Authors: Waltz, F. / Lehner, P.A. / Van der Stappen, P. / Kater, L. / Pfeffer, S. / Engel, B.D. | |||||||||||||||
| History |
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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 | 9tvu.cif.gz | 3.9 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9tvu.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9tvu.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tv/9tvu ftp://data.pdbj.org/pub/pdb/validation_reports/tv/9tvu | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 56352MC C: citing same article ( M: map data used to model this data |
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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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| 1 |
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Components
+Protein , 21 types, 21 molecules 067FHJLPRUVXZafmtuxwe
-RNA chain , 5 types, 5 molecules 35142
| #2: RNA chain | Mass: 38858.949 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #3: RNA chain | Mass: 15149.069 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #53: RNA chain | Mass: 769308.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #54: RNA chain | Mass: 88325.664 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #55: RNA chain | Mass: 476372.562 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-50S ribosomal protein ... , 2 types, 2 molecules 8Y
| #6: Protein | Mass: 12106.231 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #51: Protein | Mass: 14777.946 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Large ribosomal subunit protein ... , 15 types, 15 molecules 9BCDEGIKMNOQSTW
| #7: Protein/peptide | Mass: 4273.327 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #8: Protein | Mass: 30955.770 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #9: Protein | Mass: 27878.426 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 25659.525 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #11: Protein | Mass: 20267.668 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #13: Protein | Mass: 22043.705 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #15: Protein | Mass: 18562.955 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #17: Protein | Mass: 13466.755 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #19: Protein | Mass: 15500.425 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #20: Protein | Mass: 19188.451 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #21: Protein | Mass: 15818.282 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #23: Protein | Mass: 13578.073 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #25: Protein | Mass: 18959.348 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #26: Protein | Mass: 12565.778 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: first aa are absent from the sequence and modeled as polyA Source: (natural) ![]() |
| #29: Protein | Mass: 21945.557 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Small ribosomal subunit protein ... , 13 types, 13 molecules dghjklnqrsbci
| #33: Protein | Mass: 30082.121 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #35: Protein | Mass: 19163.799 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #36: Protein | Mass: 15916.647 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #37: Protein | Mass: 18736.729 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #38: Protein | Mass: 14260.867 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #39: Protein | Mass: 14637.429 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #41: Protein | Mass: 11776.143 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #44: Protein | Mass: 11767.698 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #45: Protein | Mass: 16315.782 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #46: Protein | Mass: 10463.467 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #56: Protein | Mass: 102698.477 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #57: Protein | Mass: 82015.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #59: Protein | Mass: 21062.168 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-30S ribosomal protein ... , 3 types, 3 molecules opv
| #42: Protein | Mass: 15817.261 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #43: Protein | Mass: 14474.052 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #49: Protein | Mass: 33397.238 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 2 types, 461 molecules 


| #60: Chemical | ChemComp-MG / #61: Chemical | ChemComp-K / |
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-Details
| Has ligand of interest | N |
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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: Chloroplast ribosome / Type: RIBOSOME / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.5 |
| Specimen | Conc.: 2.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid type: Quantifoil R2/1 |
| 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: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 75000 X / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 40 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: 2.52 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 225199 / Num. of class averages: 1 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||
| EM volume selection | Method: Template matching / Num. of tomograms: 129 / Num. of volumes extracted: 20883 | ||||||||||||||||||||||||||||||||
| Refinement | Highest resolution: 2.52 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||||||||||
| Refine LS restraints |
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FIELD EMISSION GUN