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Yorodumi- EMDB-1292: Structural basis of allosteric changes in the GroEL mutant Arg197... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-1292 | |||||||||
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Title | Structural basis of allosteric changes in the GroEL mutant Arg197-->Ala. | |||||||||
Map data | R197A Mutant of GroEL with 50uM ATp | |||||||||
Sample |
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Biological species | Escherichia coli (E. coli) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 25.0 Å | |||||||||
Authors | White HE / Chen S / Roseman AM / Yifrach O / Horovitz A / SAibil HR | |||||||||
Citation | Journal: Nat Struct Biol / Year: 1997 Title: Structural basis of allosteric changes in the GroEL mutant Arg197-->Ala. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_1292.map.gz | 983.4 KB | EMDB map data format | |
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Header (meta data) | emd-1292-v30.xml emd-1292.xml | 7.4 KB 7.4 KB | Display Display | EMDB header |
Images | 1292.gif | 122.8 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-1292 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-1292 | HTTPS FTP |
-Validation report
Summary document | emd_1292_validation.pdf.gz | 209.9 KB | Display | EMDB validaton report |
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Full document | emd_1292_full_validation.pdf.gz | 209 KB | Display | |
Data in XML | emd_1292_validation.xml.gz | 4.9 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-1292 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-1292 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_1292.map.gz / Format: CCP4 / Size: 1001 KB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | R197A Mutant of GroEL with 50uM ATp | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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
-Sample components
-Entire : R197A mutant of GroEL, 50uM ATP
Entire | Name: R197A mutant of GroEL, 50uM ATP |
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Components |
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-Supramolecule #1000: R197A mutant of GroEL, 50uM ATP
Supramolecule | Name: R197A mutant of GroEL, 50uM ATP / 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: Escherichia coli (E. coli) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 1 mg/mL |
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Buffer | pH: 7.5 / Details: 20 mM Tris, 10mM KCl, 8mmM MgCl2,50uM ATP |
Grid | Details: holey carbon |
Vitrification | Cryogen name: ETHANE Timed resolved state: Vitrified within 5 secs of ATP addition |
-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 |
-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 |