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Open data
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Basic information
| Entry | Database: PDB / ID: 9cpk | ||||||||||||
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| Title | D8 symmetry reconstruction of MmCPn in closed state | ||||||||||||
Components | Chaperonin | ||||||||||||
Keywords | CHAPERONE / Archaea chaperonin in closed state with ATP/AlFx | ||||||||||||
| Function / homology | Function and homology informationATP-dependent protein folding chaperone / unfolded protein binding / ATP hydrolysis activity / ATP binding / metal ion binding / identical protein binding Similarity search - Function | ||||||||||||
| Biological species | Methanococcus maripaludis (archaea) | ||||||||||||
| Method | ELECTRON MICROSCOPY / subtomogram averaging / cryo EM / Resolution: 2.56 Å | ||||||||||||
Authors | Yanyan, Z. | ||||||||||||
| Funding support | 3items
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Citation | Journal: Structure / Year: 2025Title: Cost-benefit analysis of cryogenic electron tomography subtomogram averaging of chaperonin MmCpn at near atomic resolution. Authors: Yanyan Zhao / Michael F Schmid / Wah Chiu / ![]() Abstract: Cryogenic electron microscopy single particle analysis (cryoEM-SPA) has evolved into a routine approach for determining macromolecule structures to near-atomic resolution. Cryogenic electron ...Cryogenic electron microscopy single particle analysis (cryoEM-SPA) has evolved into a routine approach for determining macromolecule structures to near-atomic resolution. Cryogenic electron tomography subtomogram averaging (cryoET-STA) toward a similar resolution, in contrast, is still under active development. Here, we use the archeal chaperonin MmCpn as a model macromolecule to quantitatively investigate the resolution limiting factors of cryoET-STA in terms of cumulative electron dose, ice thickness, subtomogram numbers, and tilt angle ranges. By delineating the feasibility and experimental factors of attaining near atomic resolution structure with cryoET-STA, especially the effect of electron damage through the tilt series and inelastic scattering at various ice thickness, we encourage a customized tilt series collection strategy for efficient throughput. This study provides a biophysical basis for the application of cryoET-STA (for highly symmetric molecules like MmCpn) toward high resolution and the rationales in using cryoET-STA to achieve an efficient outcome at the desired resolution. | ||||||||||||
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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 | 9cpk.cif.gz | 1.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9cpk.ent.gz | 1.1 MB | Display | PDB format |
| PDBx/mmJSON format | 9cpk.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9cpk_validation.pdf.gz | 2.4 MB | Display | wwPDB validaton report |
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| Full document | 9cpk_full_validation.pdf.gz | 2.5 MB | Display | |
| Data in XML | 9cpk_validation.xml.gz | 197.9 KB | Display | |
| Data in CIF | 9cpk_validation.cif.gz | 305.9 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cp/9cpk ftp://data.pdbj.org/pub/pdb/validation_reports/cp/9cpk | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 45793MC M: map data used to model this data C: citing same article ( |
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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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Components
-Protein , 1 types, 16 molecules BJKLMACDNEFGHIOP
| #1: Protein | Mass: 58290.262 Da / Num. of mol.: 16 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanococcus maripaludis (archaea) / Production host: ![]() |
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-Non-polymers , 5 types, 80 molecules 








| #2: Chemical | ChemComp-MG / #3: Chemical | ChemComp-ADP / #4: Chemical | ChemComp-AF3 / #5: Chemical | ChemComp-K / #6: Water | ChemComp-HOH / | |
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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: subtomogram averaging |
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Sample preparation
| Component | Name: Archaea chaperonin MmCpn under ATP/AlFx condition / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT |
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| Molecular weight | Value: 1 MDa / Experimental value: YES |
| Source (natural) | Organism: Methanococcus maripaludis (archaea) |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.2 |
| 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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1500 nm |
| Image recording | Electron dose: 3 e/Å2 / Avg electron dose per subtomogram: 39 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||
| Symmetry | Point symmetry: D8 (2x8 fold dihedral) | ||||||||||||||||
| 3D reconstruction | Resolution: 2.56 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 160000 / Symmetry type: POINT | ||||||||||||||||
| EM volume selection | Num. of tomograms: 500 / Num. of volumes extracted: 160000 |
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Methanococcus maripaludis (archaea)
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FIELD EMISSION GUN