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Yorodumi- EMDB-21491: Thermoplasma acidophilum 20S proteasome cryo-EM structure using a... -
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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-21491 | |||||||||
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| Title | Thermoplasma acidophilum 20S proteasome cryo-EM structure using automatic preprocessing workflow | |||||||||
Map data | Cryo-EM structure of T20S proteasome using automatic preprocessing workflow | |||||||||
Sample |
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| Biological species | ![]() Thermoplasma acidophilum (acidophilic) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.0 Å | |||||||||
Authors | Cianfrocco MA / Li Y | |||||||||
| Funding support | United States, 2 items
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Citation | Journal: Structure / Year: 2020Title: High-Throughput Cryo-EM Enabled by User-Free Preprocessing Routines. Authors: Yilai Li / Jennifer N Cash / John J G Tesmer / Michael A Cianfrocco / ![]() Abstract: Single-particle cryoelectron microscopy (cryo-EM) continues to grow into a mainstream structural biology technique. Recent developments in data collection strategies alongside new sample preparation ...Single-particle cryoelectron microscopy (cryo-EM) continues to grow into a mainstream structural biology technique. Recent developments in data collection strategies alongside new sample preparation devices herald a future where users will collect multiple datasets per microscope session. To make cryo-EM data processing more automatic and user-friendly, we have developed an automatic pipeline for cryo-EM data preprocessing and assessment using a combination of deep-learning and image-analysis tools. We have verified the performance of this pipeline on a number of datasets and extended its scope to include sample screening by the user-free assessment of the qualities of a series of datasets under different conditions. We propose that our workflow provides a decision-free solution for cryo-EM, making data preprocessing more generalized and robust in the high-throughput era as well as more convenient for users from a range of backgrounds. | |||||||||
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Structure visualization
| Movie |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_21491.map.gz | 324.8 MB | EMDB map data format | |
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| Header (meta data) | emd-21491-v30.xml emd-21491.xml | 8.1 KB 8.1 KB | Display Display | EMDB header |
| Images | emd_21491.png | 96.5 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-21491 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-21491 | HTTPS FTP |
-Validation report
| Summary document | emd_21491_validation.pdf.gz | 78.6 KB | Display | EMDB validaton report |
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| Full document | emd_21491_full_validation.pdf.gz | 77.7 KB | Display | |
| Data in XML | emd_21491_validation.xml.gz | 493 B | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-21491 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-21491 | HTTPS FTP |
-Related structure data
| Related structure data | C: citing same article ( |
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| Similar structure data |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_21491.map.gz / Format: CCP4 / Size: 347.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | Cryo-EM structure of T20S proteasome using automatic preprocessing workflow | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.88 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : T20S Proteasome
| Entire | Name: T20S Proteasome |
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| Components |
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-Supramolecule #1: T20S Proteasome
| Supramolecule | Name: T20S Proteasome / type: complex / ID: 1 / Parent: 0 |
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| Source (natural) | Organism: ![]() Thermoplasma acidophilum (acidophilic) |
| Recombinant expression | Organism: ![]() |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.8 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 53.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Startup model | Type of model: EMDB MAP EMDB ID: |
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| Final reconstruction | Applied symmetry - Point group: D7 (2x7 fold dihedral) / Resolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 45066 |
| Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
| Final angle assignment | Type: MAXIMUM LIKELIHOOD |
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About Yorodumi



Thermoplasma acidophilum (acidophilic)
Authors
United States, 2 items
Citation
UCSF Chimera









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