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- EMDB-46915: Recombinant AD-fold Quadruple Helical Filament Polymorph -

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Basic information

Entry
Database: EMDB / ID: EMD-46915
TitleRecombinant AD-fold Quadruple Helical Filament Polymorph
Map data
Sample
  • Complex: Truncated tau 287-391
KeywordsRecombinant Human Truncated Tau 287-391 200mM MgCl2 200 RPM 10mM PB DTT Condition 24a in original publication. / PROTEIN FIBRIL
Biological speciesHomo sapiens (human)
Methodhelical reconstruction / cryo EM / Resolution: 3.32 Å
AuthorsVaquer-Alicea J / Diamond MI / Kunach P
Funding support United States, 3 items
OrganizationGrant numberCountry
Cancer Prevention and Research Institute of Texas (CPRIT)RP220582 United States
National Institutes of Health/National Institute of Mental Health (NIH/NIMH)1RF1AG065407-01A1 United States
Chan Zuckerberg Initiative2018-191983 (5022) United States
CitationJournal: Sci Adv / Year: 2025
Title: Functional classification of tauopathy strains reveals the role of protofilament core residues.
Authors: Jaime Vaquer-Alicea / Victor A Manon / Vaibhav Bommareddy / Peter Kunach / Ankit Gupta / Jim Monistrol / Valerie A Perez / Hung Tri Tran / Nil Saez-Calveras / Siling Du / Sushobhna Batra / ...Authors: Jaime Vaquer-Alicea / Victor A Manon / Vaibhav Bommareddy / Peter Kunach / Ankit Gupta / Jim Monistrol / Valerie A Perez / Hung Tri Tran / Nil Saez-Calveras / Siling Du / Sushobhna Batra / Daniel Stoddard / Charles L White / Lukasz A Joachimiak / Sarah H Shahmoradian / Marc I Diamond /
Abstract: Distinct tau amyloid assemblies underlie diverse tauopathies but defy rapid classification. Cell and animal experiments indicate tau functions as a prion, as different strains propagated in cells ...Distinct tau amyloid assemblies underlie diverse tauopathies but defy rapid classification. Cell and animal experiments indicate tau functions as a prion, as different strains propagated in cells cause unique, transmissible neuropathology after inoculation. Strain amplification requires compatibility of the monomer and amyloid template. We used cryo-electron microscopy to study one cell-based yellow fluorescent protein (YFP)-tagged strain, resolving its amyloid nature. We then used sequential alanine (Ala) substitution (scan) within tau repeat domain (RD) to measure incorporation to preexisting tau RD-YFP aggregates. This robustly discriminated strains, defining sequences critical for monomer incorporation. We then created 3R/4R or 4R wild-type RD (amino acids 246 to 408) biosensors. Ala scan of recombinant tau seeds with the Alzheimer's disease (AD) fold matched that of AD homogenate. We scanned 22 brain lysates comprising four tauopathies. This clustered cases by neuropathological syndrome, revealed the role of amino acids in protofilament folds, and allowed strain discrimination based on amino acid requirements for prion replication.
History
DepositionSep 5, 2024-
Header (metadata) releaseMar 12, 2025-
Map releaseMar 12, 2025-
UpdateMar 12, 2025-
Current statusMar 12, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_46915.png

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Map

FileDownload / File: emd_46915.map.gz / Format: CCP4 / Size: 149.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

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AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 340 pix.
= 282.2 Å		0.83 Å/pix.
x 340 pix.
= 282.2 Å		0.83 Å/pix.
x 340 pix.
= 282.2 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.83 Å
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Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0075
Minimum - Maximum-0.013569611 - 0.031425454
Average (Standard dev.)0.0004540715 (±0.0022461375)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions340340340
Spacing340340340
CellA=B=C: 282.19998 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_46915_msk_1.map
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Additional map: #1

Fileemd_46915_additional_1.map
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Half map: #1

Fileemd_46915_half_map_1.map
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Half map: #2

Fileemd_46915_half_map_2.map
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Sample components

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Entire : Truncated tau 287-391

EntireName: Truncated tau 287-391
Components
  • Complex: Truncated tau 287-391

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Supramolecule #1: Truncated tau 287-391

SupramoleculeName: Truncated tau 287-391 / type: complex / ID: 1 / Parent: 0
Source (natural)Organism: Homo sapiens (human)

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Experimental details

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Structure determination

Methodcryo EM
Processinghelical reconstruction
Aggregation statefilament

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Sample preparation

Concentration10 mg/mL
BufferpH: 7.4 / Details: 10mM Phosphate Buffer 10mM DTT 200mM MgCl2
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 293 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 57.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 105000
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Helical parameters - Δz: 2.372 Å
Applied symmetry - Helical parameters - Δ&Phi: 179.479 °
Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric)
Resolution.type: BY AUTHOR / Resolution: 3.32 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 4.0) / Number images used: 20671
Startup modelType of model: NONE
Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

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