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- EMDB-47092: Recombinant Truncated Tau 266-391 fibrillized in NaCl Second Polymorph -

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Basic information

Entry
Database: EMDB / ID: EMD-47092
TitleRecombinant Truncated Tau 266-391 fibrillized in NaCl Second Polymorph
Map data
Sample
  • Complex: Truncated tau 266-391
KeywordsRecombinant Human Truncated Tau 266-391 200mM NaCl 200 RPM 10mM PB DTT Type 44a Filament in original publication (7QKW). / PROTEIN FIBRIL
Biological speciesHomo sapiens (human)
Methodhelical reconstruction / cryo EM / Resolution: 4.41 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 19, 2024-
Header (metadata) releaseNov 13, 2024-
Map releaseNov 13, 2024-
UpdateMar 5, 2025-
Current statusMar 5, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_47092.png

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Map

FileDownload / File: emd_47092.map.gz / Format: CCP4 / Size: 149.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

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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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Contour LevelBy AUTHOR: 0.01
Minimum - Maximum-0.0049320804 - 0.02153665
Average (Standard dev.)0.000489789 (±0.0019648543)
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_47092_msk_1.map
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Additional map: #1

Fileemd_47092_additional_1.map
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Half map: #1

Fileemd_47092_half_map_1.map
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Half map: #2

Fileemd_47092_half_map_2.map
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Sample components

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Entire : Truncated tau 266-391

EntireName: Truncated tau 266-391
Components
  • Complex: Truncated tau 266-391

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Supramolecule #1: Truncated tau 266-391

SupramoleculeName: Truncated tau 266-391 / 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 NaCl
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 opticsIllumination 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: 4.82 Å
Applied symmetry - Helical parameters - Δ&Phi: -0.93 °
Applied symmetry - Helical parameters - Axial symmetry: C2 (2 fold cyclic)
Resolution.type: BY AUTHOR / Resolution: 4.41 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 142881
Startup modelType of model: NONE
Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementProtocol: AB INITIO MODEL

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