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- EMDB-1291: Structural basis of allosteric changes in the GroEL mutant Arg197... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-1291 | |||||||||
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Title | Structural basis of allosteric changes in the GroEL mutant Arg197-->Ala. | |||||||||
![]() | GroEL R197A mutant | |||||||||
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Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 25.0 Å | |||||||||
![]() | White HE / Chen S / Roseman AM / Yifrach O / Horovitz A / SAibil HR | |||||||||
![]() | ![]() Title: Structural basis of allosteric changes in the GroEL mutant Arg197-->Ala. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 981.3 KB | ![]() | |
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Header (meta data) | ![]() ![]() | 7.3 KB 7.3 KB | Display Display | ![]() |
Images | ![]() | 131.5 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 203.3 KB | Display | ![]() |
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Full document | ![]() | 202.5 KB | Display | |
Data in XML | ![]() | 4.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | GroEL R197A mutant | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 5.6 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 : R197A mutant of GroEL
Entire | Name: R197A mutant of GroEL |
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Components |
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-Supramolecule #1000: R197A mutant of GroEL
Supramolecule | Name: R197A mutant of GroEL / type: sample / ID: 1000 / Oligomeric state: 14-mer / Number unique components: 1 |
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-Macromolecule #1: R197A mutant of GroEL
Macromolecule | Name: R197A mutant of GroEL / type: protein_or_peptide / ID: 1 / Details: MUTANT / Number of copies: 1 / Oligomeric state: 14-mer / Recombinant expression: Yes |
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Source (natural) | Organism: ![]() ![]() |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 1 mg/mL |
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Buffer | pH: 7.5 / Details: 20 mM Tris, 10mM KCl, 8mmM MgCl2, |
Grid | Details: holey carbon |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | JEOL 1200EX |
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Image recording | Category: FILM / Film or detector model: AGFA SCIENTA FILM / Digitization - Scanner: OTHER / Digitization - Sampling interval: 10 µm |
Electron beam | Acceleration voltage: 120 kV / Electron source: TUNGSTEN HAIRPIN |
Electron optics | Illumination mode: OTHER / Imaging mode: OTHER |
Sample stage | Specimen holder: Eucentric / Specimen holder model: OTHER |
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Image processing
Final reconstruction | Applied symmetry - Point group: C7 (7 fold cyclic) / Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 25.0 Å / Software - Name: SPIDER |
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-Atomic model buiding 1
Details | Manual fitting in O of an apical domain of GroEL |
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Refinement | Protocol: RIGID BODY FIT |