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- EMDB-7522: cryo-EM reconstruction of microtubule-bound full-length Tau -

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Basic information

Entry
Database: EMDB / ID: 7522
Titlecryo-EM reconstruction of microtubule-bound full-length Tau
Map datafull-length tau bound to microtubules
SampleTernary complex of alpha-beta tubulin with wildtype (full-length) tau:
full-length (Wildtype) tau / alpha-tubulin / beta-tubulinTubulin
SourceHomo sapiens (human) / Sus scrofa (pig)
Methodhelical reconstruction / cryo EM / 4.1 Å resolution
AuthorsNogales E / Hejab NMA / Kellogg EH
CitationJournal: Science / Year: 2018
Title: Near-atomic model of microtubule-tau interactions.
Authors: Elizabeth H Kellogg / Nisreen M A Hejab / Simon Poepsel / Kenneth H Downing / Frank DiMaio / Eva Nogales
Abstract: Tau is a developmentally regulated axonal protein that stabilizes and bundles microtubules (MTs). Its hyperphosphorylation is thought to cause detachment from MTs and subsequent aggregation into ...Tau is a developmentally regulated axonal protein that stabilizes and bundles microtubules (MTs). Its hyperphosphorylation is thought to cause detachment from MTs and subsequent aggregation into fibrils implicated in Alzheimer's disease. It is unclear which tau residues are crucial for tau-MT interactions, where tau binds on MTs, and how it stabilizes them. We used cryo-electron microscopy to visualize different tau constructs on MTs and computational approaches to generate atomic models of tau-tubulin interactions. The conserved tubulin-binding repeats within tau adopt similar extended structures along the crest of the protofilament, stabilizing the interface between tubulin dimers. Our structures explain the effect of phosphorylation on MT affinity and lead to a model of tau repeats binding in tandem along protofilaments, tethering together tubulin dimers and stabilizing polymerization interfaces.
DateDeposition: Mar 6, 2018 / Header (metadata) release: Apr 11, 2018 / Map release: Jan 16, 2019 / Last update: Jan 16, 2019

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 1.26
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 1.26
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_7522.png

Downloads & links

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Map

Fileemd_7522.map.gz (map file in CCP4 format, 536871 KB)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
512 pix
1.32 Å/pix.
= 675.84 Å		512 pix
1.32 Å/pix.
= 675.84 Å		512 pix
1.32 Å/pix.
= 675.84 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.32 Å
Density

Histogram

Histogram (log scale)
Contour Level:1.26 (by author), 1.26 (movie #1):
Minimum - Maximum-4.0204773 - 7.7885756
Average (Standard dev.)0.021324087 (0.41342536)
Details

EMDB XML:

Space Group Number1
Map Geometry
Axis orderXYZ
Dimensions512512512
Origin0.00.00.0
Limit511.0511.0511.0
Spacing512512512
CellA=B=C: 675.84 Å
α=β=γ: 90.0 deg.

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.321.321.32
M x/y/z512512512
origin x/y/z0.0000.0000.000
length x/y/z675.840675.840675.840
α/β/γ90.00090.00090.000
start NX/NY/NZ
NX/NY/NZ
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS512512512
D min/max/mean-4.0207.7890.021

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Supplemental data

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Sample components

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Entire Ternary complex of alpha-beta tubulin with wildtype (full-length) tau

EntireName: Ternary complex of alpha-beta tubulin with wildtype (full-length) tau
Number of components: 4

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Component #1: protein, Ternary complex of alpha-beta tubulin with wildtype (ful...

ProteinName: Ternary complex of alpha-beta tubulin with wildtype (full-length) tau
Recombinant expression: No
SourceSpecies: Homo sapiens (human)

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Component #2: protein, full-length (Wildtype) tau

ProteinName: full-length (Wildtype) tau / Recombinant expression: No
SourceSpecies: Homo sapiens (human)
Source (engineered)Expression System: Escherichia coli (E. coli)

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Component #3: protein, alpha-tubulin

ProteinName: alpha-tubulin / Recombinant expression: No
SourceSpecies: Sus scrofa (pig)

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Component #4: protein, beta-tubulin

ProteinName: beta-tubulinTubulin / Recombinant expression: No
SourceSpecies: Sus scrofa (pig)

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Experimental details

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Sample preparation

SpecimenSpecimen state: filament / Method: cryo EM
Helical parametersAxial symmetry: C1 (asymmetric) / Delta z: 8.63 Å / Delta phi: -25.75 deg.
Sample solutionSpecimen conc.: 0.5 mg/ml / pH: 6.8
Support filmunspecified
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 310.15 K / Humidity: 100 %
Details: blot force 10 pN, 6 second blot time. used C-flat 1.2/1.3 holey grids. First 2 uL of microtubules were adhered to grid for 30 seconds, followed by 2 4 uL washes with 30 second incubation for each wash..

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Electron microscopy imaging

ImagingMicroscope: FEI TITAN
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 27.5 e/Å2 / Illumination mode: FLOOD BEAM
LensMagnification: 27500.0 X (nominal) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 1000.0 - 2500.0 nm
Specimen HolderModel: GATAN LIQUID NITROGEN
CameraDetector: GATAN K2 SUMMIT (4k x 4k)

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Image acquisition

Image acquisitionNumber of digital images: 361

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Image processing

ProcessingMethod: helical reconstruction / Details: used motioncorr to correct for beam-induced motion
3D reconstructionAlgorithm: FOURIER SPACE / Software: FREALIGN / Resolution: 4.1 Å / Resolution method: FSC 0.143 CUT-OFF

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