|Entry||Database: PDB / ID: 6ehl|
|Title||Model of the Ebola virus nucleoprotein in recombinant nucleocapsid-like assemblies|
|Keywords||VIRUS LIKE PARTICLE / nucleocapsid|
|Function / homology||Ebola nucleoprotein / Ebola nucleoprotein / viral RNA genome packaging / helical viral capsid / host cell cytoplasm / viral nucleocapsid / RNA binding / Nucleoprotein|
Function and homology information
|Specimen source||Zaire ebolavirus|
|Method||ELECTRON MICROSCOPY / subtomogram averaging / cryo EM / 6.6 Å resolution|
|Authors||Wan, W. / Kolesnikova, L. / Clarke, M. / Koehler, A. / Noda, T. / Becker, S. / Briggs, J.A.G.|
|Citation||Journal: Nature / Year: 2017|
Title: Structure and assembly of the Ebola virus nucleocapsid.
Authors: William Wan / Larissa Kolesnikova / Mairi Clarke / Alexander Koehler / Takeshi Noda / Stephan Becker / John A G Briggs
SummaryFull reportAbout validation report
|Date||Deposition: Sep 13, 2017 / Release: Nov 8, 2017|
|Structure viewer||Molecule: |
Downloads & links
|#1: Protein/peptide|| |
Mass: 83387.500 Da / Num. of mol.: 1 / Mutation: Truncation mutant (residues 1-450) / Source: (gene. exp.) Zaire ebolavirus (strain Mayinga-76) / Strain: Mayinga-76 / Gene: NP / Cell line (production host): HEK-293T / Production host: Homo sapiens (human) / References: UniProt: P18272
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: HELICAL ARRAY / Reconstruction method: subtomogram averaging|
|Component||Name: Ebola virus - Mayinga, Zaire, 1976 / Type: VIRUS / Entity ID: 1 / Source: RECOMBINANT|
|Source (natural)||Organism: Ebola virus - Mayinga, Zaire, 1976|
|Source (recombinant)||Cell: HEK 293T / Organism: Homo sapiens (human)|
|Details of virus||Empty: NO / Enveloped: NO / Virus isolate: STRAIN / Virus type: VIRUS-LIKE PARTICLE|
|Virus shell||Name: NucleocapsidCapsid / Diameter: 280 nm|
|Buffer solution||pH: 7.4|
|Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Specimen support||Grid material: COPPER / Grid mesh size: 300 / Grid type: C-flat 2/1 3C|
|Vitrification||Instrument: FEI VITROBOT MARK II / Cryogen name: ETHANE / Humidity: 95 %|
-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 FIELDBright-field microscopy / Nominal magnification: 81000 / Nominal defocus max: 4500 nm / Nominal defocus min: 2000 nm / Cs: 2.7 mm / C2 aperture diameter: 5 mm / Alignment procedure: ZEMLIN TABLEAU|
|Specimen holder||Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Image recording||Average exposure time: 1 sec. / Electron dose: 2.4 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Number of grids imaged: 1|
|EM imaging optics||Energyfilter name: Gatan Quantum 967 LS / Energyfilter upper: 10 eV / Energyfilter lower: -10 eV|
|Image scans||Width: 3708 / Height: 3708 / Movie frames/image: 5 / Used frames/image: 1-5|
|Image processing||Details: Frames were aligned using K2Align software, based off the MotionCorr algorithm. Tomograms were reconstructed with IMOD, using stripwise CTF-correction and weighted back projection. Subtomogram averaging was performed using scripts derived from TOM, AV3, and DYNAMO.|
|CTF correction||Details: CTF amplitude correction was performed during the wedge-weighted subtomogram averaging step.|
Type: PHASE FLIPPING ONLY
|Symmetry||Point symmetry: C1|
|3D reconstruction||Resolution: 6.6 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 1 / Algorithm: BACK PROJECTION|
Details: Local resolution was estimated using moving window FSC calculations.
Number of class averages: 1 / Symmetry type: POINT
|EM volume selection||Details: Points along the helical axis were manually placed to define a spline. A cylindrical grid as defined at a given radius from the spline; grid spacing was chosen to provide ~4x oversampling.|
Number of tomograms: 63 / Number of volumes extracted: 488916 / Reference model: None
|Atomic model building||Details: Crystal structure was rigid-body fitted into density using Chimera. Missing regions of the structure was built using ideal secondary structures in coot. These were then flexibly fit using MDFF and NAMD.|
Ref protocol: FLEXIBLE FIT
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