|Entry||Database: EMDB / ID: 2001|
|Title||ATP-triggered molecular mechanics of the chaperonin GroEL|
|Keywords||Tetradecamer of GroEL with ATP bound in both ring|
|Source||Escherichia coli / bacteria / エシェリキア・コリ, 大腸菌 / |
|Map data||The GroEL-ATP14 Rd1-Rd3 map is one of seven maps calculated from a heterogenous sample|
|Method||single particle reconstruction, at 8.5 Å resolution|
|Authors||Clare DK / Vasishtan D / Stagg S / Quispe J / Farr GW / Topf M / Horwich AL / Saibil HR|
|Citation||Cell, 2012, 149, 113-123|
|Validation Report||PDB-ID: 4aau|
SummaryFull reportAbout validation report
|Date||Deposition: Dec 2, 2011 / Header (metadata) release: Dec 16, 2011 / Map release: Apr 17, 2012 / Last update: Oct 24, 2012|
Downloads & links
|File||emd_2001.map.gz (map file in CCP4 format, 27649 KB)|
|Projections & slices|
Images are generated by Spider package.
|Voxel size||X=Y=Z: 2.02 Å|
CCP4 map header:
-Entire GroEL-ATP14 Rd1-Rd3
|Entire||Name: GroEL-ATP14 Rd1-Rd3 / Number of components: 2|
Oligomeric State: Tetradecamer of GroEL with 14 ATP molecules bound
|Mass||Theoretical: 800 kDa / Experimental: 800 kDa|
-Component #1: protein, hsp60
|Protein||Name: hsp60 / a.k.a: GroEL / Oligomeric Details: tetradecamer / Details: ATPase Mutant, D398A / Number of Copies: 14 / Recombinant expression: Yes|
|Mass||Theoretical: 56 kDa / Experimental: 56 kDa|
|Source||Species: Escherichia coli / bacteria / エシェリキア・コリ, 大腸菌 /|
|Source (engineered)||Expression System: Escherichia coli / bacteria / エシェリキア・コリ, 大腸菌 /|
|Source (natural)||Location in cell: cytoplasm|
|External references||Gene Ontology: GO: 0042026 / InterPro: InterPro: 002423|
-Component #2: ligand, ATP
|Ligand||Name: ATP / a.k.a: ATP / Details: ATP is bound to all 14 subunits / Recombinant expression: No|
|Mass||Theoretical: 0.55 kDa / Experimental: 0.55 kDa|
|Source||Species: Synthetic construct|
|Sample solution||Specimen conc.: 4 mg/ml|
Buffer solution: 50 mM Tris-HCl pH 7.4, 50 mM KCl, 10 mM MgCl2 and 200uM ATP
|Support film||cflat grids r2/2|
|Vitrification||Instrument: FEI VITROBOT / Cryogen name: ETHANE / Temperature: 95 K / Humidity: 100 % / Method: grids were blotted for 2-3 seconds / Time resolved state: vitrified within 30 seconds / Details: Vitrification instrument: Vitrobot|
-Electron microscopy imaging
Model: Tecnai F20 / Image courtesy: FEI Company
|Imaging||Microscope: FEI TECNAI F20 / Details: The data was collected with leginon at SCRIPPS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 120 kV / Electron dose: 15 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 148500 X (calibrated) / Cs: 2 mm / Imaging mode: BRIGHT FIELD / Defocus: 700 - 3500 nm|
|Specimen Holder||Holder: Eucentric / Model: GATAN LIQUID NITROGEN / Temperature: 95 K ( 95 - 95 K)|
|Camera||Detector: GATAN ULTRASCAN 4000 (4k x 4k)|
|Processing||Method: single particle reconstruction / Number of projections: 6500|
Details: The particles were automatically picked using FindEM
Applied symmetry: C7 (7 fold cyclic)
|3D reconstruction||Algorithm: projection matching / Euler angles: theta 80-100, phi 0-51.42 / Software: SPIDER, IMAGIC / CTF correction: each particle was phase flipped / Details: SIRT was used to reconstruct the final map / Resolution: 8.5 Å / Resolution method: FSC 0.5|
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