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- EMDB-57273: AD fold in mouse injected with seeds of AD -

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ID or keywords:

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Basic information

Entry
Database: EMDB / ID: EMD-57273
TitleAD fold in mouse injected with seeds of AD
Map dataSharpened map
Sample
  • Complex: Tau filament with the AD fold from mouse seeded by human AD tau seeds
    • Protein or peptide: Isoform Tau-A of Microtubule-associated protein tau
KeywordsAmyloid / prion / tau / Alzheimer's Disease. / STRUCTURAL PROTEIN
Function / homology
Function and homology information


Caspase-mediated cleavage of cytoskeletal proteins / negative regulation of intracellular transport / negative regulation of tubulin deacetylation / positive regulation of long-term synaptic depression / PKR-mediated signaling / axon extension / axo-dendritic transport / adult walking behavior / intrinsic apoptotic signaling pathway in response to oxidative stress / mitochondrion transport along microtubule ...Caspase-mediated cleavage of cytoskeletal proteins / negative regulation of intracellular transport / negative regulation of tubulin deacetylation / positive regulation of long-term synaptic depression / PKR-mediated signaling / axon extension / axo-dendritic transport / adult walking behavior / intrinsic apoptotic signaling pathway in response to oxidative stress / mitochondrion transport along microtubule / negative regulation of protein localization to mitochondrion / neurofibrillary tangle / microtubule lateral binding / tubulin complex / positive regulation of protein localization to synapse / regulation of microtubule-based movement / intracellular distribution of mitochondria / lipoprotein particle binding / microtubule polymerization / negative regulation of mitochondrial membrane potential / apolipoprotein binding / protein polymerization / main axon / regulation of microtubule polymerization or depolymerization / axoneme / negative regulation of mitochondrial fission / axolemma / glial cell projection / mRNA transport / axonal growth cone / positive regulation of axon extension / positive regulation of microtubule polymerization / regulation of cellular response to heat / positive regulation of protein localization / positive regulation of superoxide anion generation / supramolecular fiber organization / heat shock protein binding / regulation of calcium-mediated signaling / somatodendritic compartment / response to nutrient / synapse assembly / axonogenesis / nuclear periphery / enzyme inhibitor activity / protein phosphatase 2A binding / regulation of microtubule cytoskeleton organization / regulation of autophagy / Hsp90 protein binding / positive regulation of neuron projection development / protein homooligomerization / SH3 domain binding / synapse organization / response to lead ion / microtubule cytoskeleton organization / cytoplasmic side of plasma membrane / neuron migration / memory / neuron projection development / cytoplasmic ribonucleoprotein granule / growth cone / protein-folding chaperone binding / microtubule cytoskeleton / cell body / microtubule binding / amyloid fibril formation / microtubule / learning or memory / neuron projection / postsynaptic density / membrane raft / negative regulation of gene expression / axon / neuronal cell body / DNA damage response / dendrite / protein kinase binding / protein-containing complex binding / enzyme binding / DNA binding / extracellular region / identical protein binding / nucleus / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Microtubule-associated protein Tau / Microtubule associated protein, tubulin-binding repeat / Tau and MAP protein, tubulin-binding repeat / Tau and MAP proteins tubulin-binding repeat signature. / Tau and MAP proteins tubulin-binding repeat profile. / :
Similarity search - Domain/homology
Microtubule-associated protein tau
Similarity search - Component
Biological speciesMus (mice) / Mus musculus (house mouse)
Methodhelical reconstruction / cryo EM / Resolution: 3.6 Å
AuthorsLovestam SL / Scheres SHW / Goedert M
Funding support United Kingdom, 1 items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom) United Kingdom
CitationJournal: To Be Published
Title: Prion-like transmission of human tau strains in the mouse brain
Authors: Lovestam S / Scheres SHW / Goeder M / Hasegawa M
History
DepositionMar 27, 2026-
Header (metadata) releaseMay 27, 2026-
Map releaseMay 27, 2026-
UpdateMay 27, 2026-
Current statusMay 27, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_57273.png

Downloads & links

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Map

FileDownload / File: emd_57273.map.gz / Format: CCP4 / Size: 27 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSharpened map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.49 Å/pix.
x 192 pix.
= 285.696 Å		1.49 Å/pix.
x 192 pix.
= 285.696 Å		1.49 Å/pix.
x 192 pix.
= 285.696 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.488 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.017
Minimum - Maximum-0.04054061 - 0.081556305
Average (Standard dev.)0.0008390014 (±0.0043275817)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions192192192
Spacing192192192
CellA=B=C: 285.696 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Half map 1

Fileemd_57273_half_map_1.map
AnnotationHalf map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map 2

Fileemd_57273_half_map_2.map
AnnotationHalf map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Tau filament with the AD fold from mouse seeded by human AD tau seeds

EntireName: Tau filament with the AD fold from mouse seeded by human AD tau seeds
Components
  • Complex: Tau filament with the AD fold from mouse seeded by human AD tau seeds
    • Protein or peptide: Isoform Tau-A of Microtubule-associated protein tau

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Supramolecule #1: Tau filament with the AD fold from mouse seeded by human AD tau seeds

SupramoleculeName: Tau filament with the AD fold from mouse seeded by human AD tau seeds
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Mus (mice)

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Macromolecule #1: Isoform Tau-A of Microtubule-associated protein tau

MacromoleculeName: Isoform Tau-A of Microtubule-associated protein tau / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 44.961766 KDa
SequenceString: MADPRQEFDT MEDHAGDYTL LQDQEGDMDH GLKESPPQPP ADDGAEEPGS ETSDAKSTPT AEDVTAPLVD ERAPDKQAAA QPHTEIPEG ITAEEAGIGD TPNQEDQAAG HVTQARVASK DRTGNDEKKA KGADGKTGAK IATPRGAASP AQKGTSNATR I PAKTTPSP ...String:
MADPRQEFDT MEDHAGDYTL LQDQEGDMDH GLKESPPQPP ADDGAEEPGS ETSDAKSTPT AEDVTAPLVD ERAPDKQAAA QPHTEIPEG ITAEEAGIGD TPNQEDQAAG HVTQARVASK DRTGNDEKKA KGADGKTGAK IATPRGAASP AQKGTSNATR I PAKTTPSP KTPPGSGEPP KSGERSGYSS PGSPGTPGSR SRTPSLPTPP TREPKKVAVV RTPPKSPSAS KSRLQTAPVP MP DLKNVRS KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI VYKPVDLSKV TSKCGSLGNI HHK PGGGQV EVKSEKLDFK DRVQSKIGSL DNITHVPGGG NKKIETHKLT FRENAKAKTD HGAEIVYKSP VVSGDTSPRH LSNV SSTGS IDMVDSPQLA TLADEVSASL AKQGL

UniProtKB: Microtubule-associated protein tau

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Experimental details

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Structure determination

Methodcryo EM
Processinghelical reconstruction
Aggregation statefilament

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Sample preparation

BufferpH: 7.2
GridModel: Quantifoil / Material: GOLD / Mesh: 300
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Helical parameters - Δz: 2.42 Å
Applied symmetry - Helical parameters - Δ&Phi: 179.446 °
Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric)
Resolution.type: BY AUTHOR / Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 5.1) / Number images used: 90623
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER / Details: De novo
Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

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