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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-6245 | |||||||||
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| Title | Thermoplasma acidophilum 20S proteasome | |||||||||
Map data | Thermoplasma acidophilum 20S proteasome. Reconstruction determined from the first 5,000 particles of a dataset used to calculate map EMD-5623. | |||||||||
Sample |
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Keywords | T. acidophilum 20S proteasome | |||||||||
| Biological species | ![]() Thermoplasma acidophilum (acidophilic) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 4.1 Å | |||||||||
Authors | Li X / Cheng Y | |||||||||
Citation | Journal: Nat Methods / Year: 2015Title: Atomic-accuracy models from 4.5-Å cryo-electron microscopy data with density-guided iterative local refinement. Authors: Frank DiMaio / Yifan Song / Xueming Li / Matthias J Brunner / Chunfu Xu / Vincent Conticello / Edward Egelman / Thomas Marlovits / Yifan Cheng / David Baker / ![]() Abstract: We describe a general approach for refining protein structure models on the basis of cryo-electron microscopy maps with near-atomic resolution. The method integrates Monte Carlo sampling with local ...We describe a general approach for refining protein structure models on the basis of cryo-electron microscopy maps with near-atomic resolution. The method integrates Monte Carlo sampling with local density-guided optimization, Rosetta all-atom refinement and real-space B-factor fitting. In tests on experimental maps of three different systems with 4.5-Å resolution or better, the method consistently produced models with atomic-level accuracy largely independently of starting-model quality, and it outperformed the molecular dynamics-based MDFF method. Cross-validated model quality statistics correlated with model accuracy over the three test systems. | |||||||||
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Structure visualization
| Movie |
Movie viewer |
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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_6245.map.gz | 59.1 MB | EMDB map data format | |
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| Header (meta data) | emd-6245-v30.xml emd-6245.xml | 8.7 KB 8.7 KB | Display Display | EMDB header |
| Images | 400_6245.gif 80_6245.gif | 64.6 KB 5.2 KB | ||
| Others | emd_6245_half_map_1.map.gz emd_6245_half_map_2.map.gz | 56.7 MB 56.7 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-6245 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-6245 | HTTPS FTP |
-Validation report
| Summary document | emd_6245_validation.pdf.gz | 78.8 KB | Display | EMDB validaton report |
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| Full document | emd_6245_full_validation.pdf.gz | 77.9 KB | Display | |
| Data in XML | emd_6245_validation.xml.gz | 493 B | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-6245 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-6245 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_6245.map.gz / Format: CCP4 / Size: 62.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | Thermoplasma acidophilum 20S proteasome. Reconstruction determined from the first 5,000 particles of a dataset used to calculate map EMD-5623. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.2156 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Supplemental map: emd 6245 half map 1.map
| File | emd_6245_half_map_1.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
-Supplemental map: emd 6245 half map 2.map
| File | emd_6245_half_map_2.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Thermoplasma acidophilum 20S proteasome
| Entire | Name: Thermoplasma acidophilum 20S proteasome |
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| Components |
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-Supramolecule #1000: Thermoplasma acidophilum 20S proteasome
| Supramolecule | Name: Thermoplasma acidophilum 20S proteasome / type: sample / ID: 1000 / Details: The sample was monodisperse. / Oligomeric state: 28-mer / Number unique components: 1 |
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| Molecular weight | Experimental: 700 KDa |
-Macromolecule #1: Thermoplasma acidophilum 20S proteasome
| Macromolecule | Name: Thermoplasma acidophilum 20S proteasome / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Oligomeric state: 28-mer / Recombinant expression: Yes |
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| Source (natural) | Organism: ![]() Thermoplasma acidophilum (acidophilic) |
| Molecular weight | Experimental: 700 KDa |
| 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
| Grid | Details: Quantifoil |
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| Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK III |
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Electron microscopy
| Microscope | FEI POLARA 300 |
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| Date | Jan 1, 2012 |
| Image recording | Category: CCD / Film or detector model: GATAN K2 (4k x 4k) / Average electron dose: 20 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.0 mm / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.9 µm / Nominal magnification: 31000 |
| Sample stage | Specimen holder model: SIDE ENTRY, EUCENTRIC |
| Experimental equipment | ![]() Model: Tecnai Polara / Image courtesy: FEI Company |
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Image processing
| Details | FREALIGN |
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| Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.1 Å / Resolution method: OTHER / Number images used: 5000 |
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Keywords
Thermoplasma acidophilum (acidophilic)
Authors
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