|Entry||Database: PDB / ID: 5o3o|
|Title||Pronase-treated paired helical filament in Alzheimer's disease brain|
|Descriptor||Microtubule-associated protein tau|
|Keywords||PROTEIN FIBRIL / TAU / AMYLOID / CROSS-BETA / BETA-HELIX|
|Specimen source||Homo sapiens / human|
|Method||Electron microscopy (3.5 Å resolution / Tissue / Helical)|
|Authors||Fitzpatrick, A.W.P. / Falcon, B. / He, S. / Murzin, A.G. / Murshudov, G. / Garringer, H.G. / Crowther, R.A. / Ghetti, B. / Goedert, M. / Scheres, S.H.W.|
|Citation||Nature, 2017, 547, 185-190|
SummaryFull reportAbout validation report
|Date||Deposition: May 24, 2017 / Release: Jul 26, 2017|
Downloads & links
A: Microtubule-associated protein tau
B: Microtubule-associated protein tau
C: Microtubule-associated protein tau
D: Microtubule-associated protein tau
E: Microtubule-associated protein tau
F: Microtubule-associated protein tau
G: Microtubule-associated protein tau
H: Microtubule-associated protein tau
I: Microtubule-associated protein tau
J: Microtubule-associated protein tau
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: TISSUE / Reconstruction method: HELICAL|
|Component||Name: Tau from brain / Type: TISSUE / Entity ID: 1 / Source: NATURAL|
|Source (natural)||Organism: Homo sapiens|
|Buffer solution||Details: 20 mM Tris-HCl pH 7.4 containing 100 mM NaCl / pH: 7.4|
|Specimen||Conc.: 1 mg/ml|
Details: Sarkosyl-insoluble material was extracted from grey matter of frontal and temporal cortex from the patients brain and treated with pronase, as described in the Methods section of the paper.
Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
|Specimen support||Grid material: GOLD / Grid mesh size: 300 / Grid type: Quantifoil Au R1.2/1.3|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 kelvins|
-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 / Nominal defocus max: 3000 nm / Nominal defocus min: 900 nm / Calibrated defocus min: 900 nm / Calibrated defocus max: 3000 nm / Cs: 2.7 mm / C2 aperture diameter: 70 mm / Alignment procedure: COMA FREE|
|Specimen holder||Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Image recording||Average exposure time: 0.8 sec. / Electron dose: 2.5 e/Å2|
Details: images were collected in movie-mode at 1.2 frames per second
Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Number of grids imaged: 1 / Number of real images: 523
|EM imaging optics||Energyfilter name: GIF Quantum / Energyfilter upper: 10 eV / Energyfilter lower: -10 eV|
|Image scans||Dimension width: 3710 / Dimension height: 3710 / Movie frames/image: 20 / Used frames/image: 2-20|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Helical symmerty||Angular rotation/subunit: 179.4 deg. / Axial rise/subunit: 2.36 Å / Axial symmetry: C1|
|Particle selection||Number of particles selected: 66585|
|3D reconstruction||Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 20778 / Number of class averages: 1 / Symmetry type: HELICAL|
|Atomic model building||Details: Fourier-space refinement of the complete atomic model against the paired helical filament and straight filament maps was performed in REFMAC. A stack of three consecutive monomers from each of the protofilaments was refined to preserve nearest-neighbour interactions for the middle chain.|
Overall b value: 106 / Ref protocol: AB INITIO MODEL / Ref space: RECIPROCAL / Target criteria: Fourier shell correlation
|Atomic model building||PDB-ID: 2RNM|
Pdb chain ID: A / Pdb chain residue range: 226-242
-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.
- Joachim Frank (Columbia University, New York, USA) is a pioneer of single particle reconstruction, which is the most used reconstruction method for 3DEM structures in EMDB and EM entries in PDB. And also, he is a develper of Spider, which is one of the most famous software in this field, and is used for some EM Navigor data (e.g. map projection/slice images).
- 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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