|Entry||Database: EMDB / ID: 3894|
|Title||S.aureus ClpC resting state, C2 symmetrised|
|Sample||Resting-state oligomeric complex of S. aureus ClpC|
|Source||Staphylococcus aureus / bacteria / スタフィロコッカス・アウレウス, 黄色ブドウ球菌|
|Map data||Resting state of ClpC from S. aureus. C2 symmetry applied.|
|Method||single particle reconstruction, at 8.4 Å resolution|
|Authors||Carroni M / Mogk A|
|Citation||Elife, 2017, 6|
Elife, 2017, 6 Yorodumi Papers
|Validation Report||PDB-ID: 6em8|
About validation report
|Date||Deposition: Oct 1, 2017 / Header (metadata) release: Dec 27, 2017 / Map release: Dec 27, 2017 / Last update: Dec 27, 2017|
Downloads & links
|File||emd_3894.map.gz (map file in CCP4 format, 108001 KB)|
|Projections & slices|
Images are generated by Spider package.
|Voxel size||X=Y=Z: 1.34 Å|
CCP4 map header:
|File||emd_3894_msk_1.map ( map file in CCP4 format, 108001 KB )|
|Projections & Slices|
|Data type||Image stored as Reals|
|Annotation details||Mask. Resting state of ClpC from S. aureus. C2 symmetry applied.|
|Space group number||1|
-Entire Resting-state oligomeric complex of S. aureus ClpC
|Entire||Name: Resting-state oligomeric complex of S. aureus ClpC / Number of components: 2|
|Mass||Experimental: 900 kDa|
-Component #1: protein, Resting-state oligomeric complex of S. aureus ClpC
|Protein||Name: Resting-state oligomeric complex of S. aureus ClpC / Recombinant expression: No|
|Mass||Experimental: 900 kDa|
|Source||Species: Staphylococcus aureus / bacteria / スタフィロコッカス・アウレウス, 黄色ブドウ球菌|
|Source (engineered)||Expression System: Escherichia coli / bacteria / エシェリキア・コリ, 大腸菌 /|
-Component #2: protein, ATP-dependent Clp protease ATP-binding subunit ClpC
|Protein||Name: ATP-dependent Clp protease ATP-binding subunit ClpC / Recombinant expression: No|
|Mass||Theoretical: 91.170352 kDa|
|Source (engineered)||Expression System: Staphylococcus aureus / bacteria / スタフィロコッカス・アウレウス, 黄色ブドウ球菌|
|Sample solution||pH: 7.5|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 297 K / Humidity: 100 %|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 30 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD / Defocus: 1000 - 3000 nm|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: FEI FALCON II (4k x 4k)|
|Processing||Method: single particle reconstruction / Applied symmetry: C2 (2 fold cyclic) / Number of projections: 40000|
|3D reconstruction||Software: RELION / Resolution: 8.4 Å / Resolution method: FSC 0.143 CUT-OFF|
|FSC plot (resolution assessment)|
-Atomic model buiding
-Oct 4, 2017. Three pioneers of this field were awarded Nobel Prize in Chemistry 2017
Three pioneers of this field were awarded Nobel Prize in Chemistry 2017
- Jacques Dubochet (University of Lausanne, Switzerland) is a pioneer of ice-embedding method of EM specimen (as known as cryo-EM), Most of 3DEM structures in EMDB and PDB are obtained using his method.
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- Richard Henderson (MRC Laboratory of Molecular Biology, Cambridge, UK) was determined the first biomolecule structure by EM. The first EM entry in PDB, PDB-1brd is determinedby him.
External links: The 2017 Nobel Prize in Chemistry - Press Release
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