9pgo

Cryo-EM structure of brain-derived Tau fibril from Alzheimers disease patient tissue

Method: ELECTRON MICROSCOPY Dmax: 140.4 Å Quality: GOOD

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

Microtubule-associated protein tau

OrganismNot specified

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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain A; UniProt 1–758 Chain B; UniProt 1–758 Chain C; UniProt 1–758 Chain D; UniProt 1–758 Chain E; UniProt 1–758 Chain F; UniProt 1–758 Chain G; UniProt 1–758 Chain H; UniProt 1–758 Chain I; UniProt 1–758 Chain J; UniProt 1–758 Chain K; UniProt 1–758 Chain L; UniProt 1–758 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.29 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
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–758; UniProt 1–758 Author chain B; PDBConstruct 1–758; UniProt 1–758 Author chain C; PDBConstruct 1–758; UniProt 1–758 Author chain D; PDBConstruct 1–758; UniProt 1–758 Author chain E; PDBConstruct 1–758; UniProt 1–758 Author chain F; PDBConstruct 1–758; UniProt 1–758 Author chain G; PDBConstruct 1–758; UniProt 1–758 Author chain H; PDBConstruct 1–758; UniProt 1–758 Author chain I; PDBConstruct 1–758; UniProt 1–758 Author chain J; PDBConstruct 1–758; UniProt 1–758 Author chain K; PDBConstruct 1–758; UniProt 1–758 Author chain L; PDBConstruct 1–758; UniProt 1–758

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 9pgo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9pgo
Deposition date deposition_date2025-07-08
Structure title titleCryo-EM structure of brain-derived Tau fibril from Alzheimers disease patient tissue
Keywords keywords;Tau, Neurodegeneration, fibril, patient derived, Alzheimer's Disease, Helical Reconstruction, amyloid structural protein, PROTEIN FIBRIL ;; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.87
Radius of gyration Rg (electron density) rg_electron37.69
Forward intensity I(0) i0141069000.00
Molecular weight molecular_weight95991.0 kDa
Excluded volume excluded_volume120960 ų
Envelope volume envelope_volume160210 ų
Hydration-shell volume shell_volume39089 ų
Envelope diameter envelope_diameter146.2
Shell Rg shell_rg39.11
Envelope Rg envelope_rg38.09
Shape Rg shape_rg37.66
Total Rg total_rg37.89
Total atoms total_atoms6756
Residues n_residues888
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 dmax140.4
Rg (real space) rg_real36.39
Rg uncertainty (real space) rg_real_error1.72
I(0) (real space) i0_real1.4110e+08
I(0) uncertainty (real space) i0_real_error2.7350e+06
Rg (reciprocal space) rg_reciprocal36.07
I(0) (reciprocal space) i0_reciprocal141000000.0000
Solution quality estimate total_estimate0.7549
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.3
Skewness Skewness skewness0.739
Kurtosis Kurtosis kurtosis0.293
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8516000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.439; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.508; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)