|Entry||Database: PDB / ID: 5o3l|
|Title||Paired helical filament in Alzheimer's disease brain|
|Descriptor||Microtubule-associated protein tau|
|Keywords||STRUCTURAL PROTEIN / TAU / AMYLOID / CROSS-BETA / BETA-HELIX|
|Specimen source||Homo sapiens / human|
|Method||Electron microscopy (3.4 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
Mass: 7940.141 Da / Num. of mol.: 10 / Fragment: UNP Residues 623-695 / Source: (gene. exp.) Homo sapiens / human / References: UniProt: P10636
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: TISSUE / Reconstruction method: HELICAL|
|Component||Name: Structure of Paired Helical Filaments from Alzheimer's Disease 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, 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: 0.2 sec. / Electron dose: 1.2 e/Å2|
Details: images were collected in movie-mode at 5 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: 1560
|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: 50|
|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: 214757|
|3D reconstruction||Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 23086 / 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: 105 / 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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