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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | 3D Reconstruction of PPG Matrix-Landed GroEL Protein Complexes | |||||||||
Map data | 3D Reconstruction of PPG Matrix-Landed GroEL Protein Complexes | |||||||||
Sample |
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Keywords | Matrix-Landed / CHAPERONE | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / negative staining / Resolution: 15.0 Å | |||||||||
Authors | Salome AZ / Westphall MS | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: To Be PublishedTitle: Matrix-Landing Mass Spectrometry for Electron Microscopy Imaging of Native Protein Complexes Authors: Salome AZ / Westphall MS | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_27809.map.gz | 7 MB | EMDB map data format | |
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| Header (meta data) | emd-27809-v30.xml emd-27809.xml | 7.6 KB 7.6 KB | Display Display | EMDB header |
| Images | emd_27809.png | 38.4 KB | ||
| Filedesc metadata | emd-27809.cif.gz | 3.5 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-27809 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-27809 | HTTPS FTP |
-Validation report
| Summary document | emd_27809_validation.pdf.gz | 416.3 KB | Display | EMDB validaton report |
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| Full document | emd_27809_full_validation.pdf.gz | 415.9 KB | Display | |
| Data in XML | emd_27809_validation.xml.gz | 5.4 KB | Display | |
| Data in CIF | emd_27809_validation.cif.gz | 6.1 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-27809 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-27809 | HTTPS FTP |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_27809.map.gz / Format: CCP4 / Size: 8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | 3D Reconstruction of PPG Matrix-Landed GroEL Protein Complexes | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 3.4 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : Chaperonin 60
| Entire | Name: Chaperonin 60 |
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| Components |
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-Supramolecule #1: Chaperonin 60
| Supramolecule | Name: Chaperonin 60 / type: complex / ID: 1 / Parent: 0 |
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| Source (natural) | Organism: ![]() |
-Experimental details
-Structure determination
| Method | negative staining |
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Processing | single particle reconstruction |
| Aggregation state | cell |
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Sample preparation
| Buffer | pH: 7 |
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| Staining | Type: NEGATIVE / Material: Uranyl Acetate |
| Grid | Model: Homemade / Material: COPPER / Mesh: 400 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. |
| Details | Protein complex solution was ionized and converted to gas-phase via electrospray ionization. GroEL gas-phase ions were collected for analysis. |
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Electron microscopy
| Microscope | FEI TECNAI 12 |
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| Image recording | Film or detector model: OTHER / Average electron dose: 100.0 e/Å2 / Details: NanoSprint15 MK-II 15 Mpix camera (AMT Imaging) |
| Electron beam | Acceleration voltage: 120 kV / Electron source: LAB6 |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.5 µm |
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Image processing
| Startup model | Type of model: OTHER |
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| Final reconstruction | Applied symmetry - Point group: D7 (2x7 fold dihedral) / Resolution.type: BY AUTHOR / Resolution: 15.0 Å / Resolution method: OTHER / Software - Name: cisTEM / Number images used: 20922 |
| Initial angle assignment | Type: NOT APPLICABLE |
| Final angle assignment | Type: NOT APPLICABLE |
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Keywords
Authors
United States, 1 items
Citation
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