|Entry||Database: EMDB / ID: 1960|
|Title||Symmetry-free cryo-EM map of TRiC in the nucleotide-free (apo) state|
|Keywords||TRiC/CCT / chaperonin / cryo-EM / protein folding|
|Sample||Bovine TRiC/CCT in the nucleotide-free (apo) state|
|Source||Bos taurus / mammal / bovine / Cattle /|
|Map data||symmetry-free apo-TRiC 3D reconstruction|
|Method||single particle reconstruction, at 10.5 Å resolution|
|Authors||Cong Y / Schroder GF / Meyer AS / Jakana J / Ma B / Dougherty MT / Schmid MF / Reissmann S / Levitt M / Ludtke SL / Frydman J / Chiu W|
|Citation||EMBO J., 2012, 31, 720-730|
EMBO J., 2012, 31, 720-730 Yorodumi Papers
|Validation Report||PDB-ID: 4a0o|
SummaryFull reportAbout validation report
|Date||Deposition: Sep 3, 2011 / Header (metadata) release: Feb 6, 2012 / Map release: Feb 6, 2012 / Last update: Mar 20, 2013|
Downloads & links
|File||emd_1960.map.gz (map file in CCP4 format, 11665 KB)|
|Projections & slices|
Images are generated by Spider package.
|Voxel size||X=Y=Z: 2.4 Å|
CCP4 map header:
-Entire Bovine TRiC/CCT in the nucleotide-free (apo) state
|Entire||Name: Bovine TRiC/CCT in the nucleotide-free (apo) state / Number of components: 1 / Oligomeric State: 16-mer|
|Mass||Theoretical: 1000 kDa / Experimental: 1000 kDa|
-Component #1: protein, bovine TRiC
|Protein||Name: bovine TRiC / a.k.a: TRiC or CCT / Oligomeric Details: 16-mer / Recombinant expression: No|
|Mass||Theoretical: 1000 kDa / Experimental: 1000 kDa|
|Source||Species: Bos taurus / mammal / bovine / Cattle /|
|Source (natural)||Organ or tissue: Testes|
|Sample solution||Specimen conc.: 1 mg/ml|
|Support film||200-mesh Quantifoil holey grid|
|Vitrification||Instrument: FEI VITROBOT / Cryogen name: ETHANE / Temperature: 101 K / Humidity: 100 % / Method: Two-side blotting for 1 second before plunging / Details: Vitrification instrument: FEI vitrobot|
-Electron microscopy imaging
|Imaging||Microscope: JEOL 3200FSC / Date: Oct 20, 2008|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 18 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 50000 X (nominal) / Astigmatism: objective lens astigmatism correction / Cs: 4.1 mm / Imaging mode: BRIGHT FIELD / Defocus: 1200 - 3000 nm / Energy filter: JEOL in-column omega energy filter / Energy window: 0-20 eV|
|Specimen Holder||Holder: Side entry / Model: JEOL 3200FSC CRYOHOLDER / Temperature: 101 K|
|Camera||Detector: KODAK SO-163 FILM|
|Image acquisition||Number of digital images: 700 / Scanner: NIKON SUPER COOLSCAN 9000 / Sampling size: 6.35 microns|
|Processing||Method: single particle reconstruction / Number of projections: 47151 / Applied symmetry: C1 (asymmetric)|
|3D reconstruction||Algorithm: Projection matching / Software: EMAN1.8 / CTF correction: each micrograph|
Details: A recently developed 2-D fast rotational matching (FRM2D) algorithm for image alignment, available in EMAN 1.8, was adopted in the refinement steps
Resolution: 10.5 Å / Resolution method: FSC 0.5
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External links: The 2017 Nobel Prize in Chemistry - Press Release
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