Database: EMDB / ID: 1046|
|Title||ATP-bound states of GroEL captured by cryo-electron microscopy.|
|Sample||GroES-ADP7-GroEL-ATP7 from E.coli|
|Source||Escherichia coli / bacteria /|
|Map data||GroEL with GroES and ADP bound to one ring, and ATP bound to the other ring|
|Method||single particle reconstruction, at 23.5 A resolution|
|Citation||Cell, 2001, 107, 869-879|
|Date||Deposition: Mar 13, 2003 / Header (metadata) release: May 16, 2003 / Map release: May 16, 2003 / Last update: Mar 13, 2003|
|3D viewer|| / |
Downloads & links
|File||emd_1046.map.gz (map file in CCP4 format, 8193 KB)|
|Projections & slices||Size of images: |
Images are generated by Spider package.
|Voxel size||X=Y=Z: 2.8 A|
CCP4 map header:
Entire GroES-ADP7-GroEL-ATP7 from E.coli
|Entire||Name: GroES-ADP7-GroEL-ATP7 from E.coli|
Details: The complexes were prepared by pre-forming a GroEL-GroES-ADP complex, with 100 uM ADP, then adding an excess of single ring GroEL (SR1) to trap any released GroES; then 1 mM ATP was added. Any GroEL-GroES complexes remaining have ADP in the GroES-bound ring and ATP in the other ring, modelling the in vivo ATP-binding reaction.
Oligomeric State: 14-mer / Number of components: 2
|Mass||Theoretical: 1000 kDa / Experimental: 1000 kDa|
Component #1: protein, GroEL
|Protein||Name: GroEL / a.k.a: Chaperonin 60 / Oligomeric Details: 14-mer / Number of Copies: 1 / Recombinant expression: Yes|
|Mass||Theoretical: 800 kDa / Experimental: 800 kDa|
|Source||Species: Escherichia coli / bacteria /|
|Source (engineered)||Expression System: Escherichia coli / bacteria /|
|Source (natural)||Cell: E. coli|
Component #2: protein, GroES
|Sample solution||Specimen conc.: 0.8 mg/ml|
Buffer solution: 12.5 mM HEPES, 5 mM KCl, 5 mM MgCl2, 100 uM ADP, then 2x molar excess of single ring mutant of GroEL (SR1), then 1 mM ATP just before vitrification. See sample details for an explanation of the experimental design.
|Support film||holey carbon film|
|Vitrification||Instrument: HOMEMADE PLUNGER / Cryogen name: ETHANE / Temperature: 100 K / Method: Blot for 1 second before plunging|
Time resolved state: The sample was vitrified within a few seconds of manually mixing in ATP.
Details: Vitrification instrument: self made
Electron microscopy imaging
|Imaging||Microscope: FEI TECNAI F20|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Electron dose: 20 e/A2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 50000 X (nominal) / Cs: 2 mm / Imaging mode: BRIGHT FIELD / Defocus: 900 - 3000 nm|
|Specimen Holder||Holder: Eucentric / Model: GATAN LIQUID NITROGEN / Temperature: 105 K|
|Camera||Detector: KODAK SO-163 FILM|
|Image acquisition||Number of digital images: 71 / Scanner: ZEISS SCAI / Sampling size: 14 microns / Bit depth: 8 / OD range: 1|
|Processing||Method: single particle reconstruction / Number of projections: 1448 / Applied symmetry: C7 (7 fold cyclic)|
|3D reconstruction||Algorithm: Projection matching / Software: Spider|
CTF correction: CTF multiplication and merging of 2D averages
Resolution: 23.5 A / Resolution method: FSC 0.5
Euler angles: Full coverage around a single axis, using mainly side views
Details: Filtered back projection
Atomic model buiding
|Modeling #1||Software: Manual fitting in O / Refinement protocol: rigid body / Refinement space: REAL|
Details: Protocol: Rigid body. The only movement relative to the crystal structure of GroEL-ES-ADP seen at this resolution is a twist of the free apical domains.
Input PDB model: 1AON
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