9cgz

Alzheimer's Disease Seeded Mixed 0N4R and 0N3R Tau Fibrils

Method: ELECTRON MICROSCOPY Dmax: 134.4 Å Quality: REASONABLE

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

Isoform Fetal-tau 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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–352 Chain B; UniProt 1–352 Chain C; UniProt 1–352 Chain D; UniProt 1–352 Chain E; UniProt 1–352 Chain F; UniProt 1–352 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.69 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 P10636-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–352; UniProt 1–352 Author chain B; PDBConstruct 1–352; UniProt 1–352 Author chain C; PDBConstruct 1–352; UniProt 1–352 Author chain D; PDBConstruct 1–352; UniProt 1–352 Author chain E; PDBConstruct 1–352; UniProt 1–352 Author chain F; PDBConstruct 1–352; UniProt 1–352

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 9cgz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9cgz
Deposition date deposition_date2024-07-01
Structure title titleAlzheimer's Disease Seeded Mixed 0N4R and 0N3R Tau Fibrils
Keywords keywordsTau, Amyloid, Cross-beta, Seeded-Fibril, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.90
Radius of gyration Rg (electron density) rg_electron36.03
Forward intensity I(0) i035845300.00
Molecular weight molecular_weight47473.0 kDa
Excluded volume excluded_volume59907 ų
Envelope volume envelope_volume84976 ų
Hydration-shell volume shell_volume22986 ų
Envelope diameter envelope_diameter137.4
Shell Rg shell_rg35.39
Envelope Rg envelope_rg36.49
Shape Rg shape_rg36.00
Total Rg total_rg36.06
Total atoms total_atoms6822
Residues n_residues438
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 dmax134.4
Rg (real space) rg_real34.40
Rg uncertainty (real space) rg_real_error2.15
I(0) (real space) i0_real3.5850e+07
I(0) uncertainty (real space) i0_real_error7.5650e+05
Rg (reciprocal space) rg_reciprocal34.09
I(0) (reciprocal space) i0_reciprocal35840000.0000
Solution quality estimate total_estimate0.7334
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.2
Skewness Skewness skewness0.686
Kurtosis Kurtosis kurtosis0.172
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1300000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.449; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.318; Smooth: 0.868

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)