|Entry||Database: PDB / ID: 6b3o|
|Title||Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion|
|Keywords||VIRAL PROTEIN / Coronavirus / membrane fusion / MHV / SARS / MERS|
|Specimen source||Murine coronavirus / virus|
|Method||Electron microscopy (4.1 Å resolution / Particle / Single particle)|
|Authors||Walls, A.C. / Tortorici, M.A. / Snijder, J. / Xiong, X. / Bosch, B.J. / Rey, F.A. / Veesler, D.|
|Citation||Proc. Natl. Acad. Sci. U.S.A., 2017, 114, 11157-11162|
Proc. Natl. Acad. Sci. U.S.A., 2017, 114, 11157-11162 Yorodumi Papers
SummaryFull reportAbout validation report
|Date||Deposition: Sep 22, 2017 / Release: Oct 4, 2017|
Downloads & links
A: Spike glycoprotein
B: Spike glycoprotein
C: Spike glycoprotein
Mass: 66199.094 Da / Num. of mol.: 3 / Fragment: residues 718-1252 / Source: (gene. exp.) Murine coronavirus / virus / Strain: A59 / Gene: S, 3 / Production host: Drosophila melanogaster / References: UniProt: P11224
|Sequence details||The authors state that all the differences between the sequence provided and the sequence database reference are accounted for by modifications that they made to their construct: residues 1253-1254: BiP secretion signal, residues 1253-1254: linker, residues 1255-1284: GCN4 trimerization motif, residues 1285-1290: Thrombin cleavage site, residues 1291-1300: Strep-tag|
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / Reconstruction method: SINGLE PARTICLE|
|Component||Name: Mouse hepatitis virus spike glycoprotein (S2 subunit) in the postfusion conformation|
Type: COMPLEX / Entity ID: 1 / Source: RECOMBINANT
|Molecular weight||Value: 0.18 deg. / Units: MEGADALTONS / Experimental value: NO|
|Source (natural)||Organism: Murine hepatitis virus|
|Source (recombinant)||Organism: Drosophila melanogaster|
|Buffer solution||pH: 7.5|
|Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Specimen support||Grid material: COPPER / Grid mesh size: 400 / Grid type: Protochips C-flat|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Microscope model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELD|
|Image recording||Electron dose: 60 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k)|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Symmetry||Point symmetry: C3|
|3D reconstruction||Resolution: 4.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 106000 / Symmetry type: POINT|
|Atomic model building||Ref protocol: AB INITIO MODEL / Ref space: REAL|
-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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