9r2h

Tau filaments seeded by AD homogenate using 0N3R C322S

Method: ELECTRON MICROSCOPY Dmax: 101.3 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Isoform Tau-D of Microtubule-associated protein tau

Homo sapiens

UniProt P10636

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 248–383 Chain B; UniProt 248–383 Chain C; UniProt 248–383 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

248 other PDB entries and 270 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TAU_HUMAN
Isoform P10636-6
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–136; UniProt 248–383 Author chain B; PDBConstruct 1–136; UniProt 248–383 Author chain C; PDBConstruct 1–136; UniProt 248–383

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 9r2h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9r2h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9r2h
Deposition date deposition_date2025-04-30
Structure title titleTau filaments seeded by AD homogenate using 0N3R C322S
Keywords keywords;MAPT, Tau, Alzheimer's Disease, RT-QuiC, PROTEIN FIBRIL ;; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier29.40
Radius of gyration Rg (electron density) rg_electron29.29
Forward intensity I(0) i026026100.00
Molecular weight molecular_weight37680.0 kDa
Excluded volume excluded_volume46607 ų
Envelope volume envelope_volume65092 ų
Hydration-shell volume shell_volume20475 ų
Envelope diameter envelope_diameter97.7
Shell Rg shell_rg33.16
Envelope Rg envelope_rg29.35
Shape Rg shape_rg29.30
Total Rg total_rg29.68
Total atoms total_atoms5316
Residues n_residues357
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax101.3
Rg (real space) rg_real29.65
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real2.6030e+07
I(0) uncertainty (real space) i0_real_error4.1580e+05
Rg (reciprocal space) rg_reciprocal29.55
I(0) (reciprocal space) i0_reciprocal26020000.0000
Solution quality estimate total_estimate0.8622
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary28.1
Skewness Skewness skewness0.462
Kurtosis Kurtosis kurtosis-0.428
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1393000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.851; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.738; Smooth: 0.915

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)