7qkh

In vitro assembled 258-391 tau filaments with sodium azide, (41a)

Method: ELECTRON MICROSCOPY Dmax: 120.1 Å Quality: REASONABLE

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

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 1–441 Chain B; UniProt 1–441 Chain C; UniProt 1–441 Chain D; UniProt 1–441 Chain E; UniProt 1–441 Chain G; UniProt 1–441 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.17 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 P10636-8
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–441; UniProt 1–441 Author chain B; PDBConstruct 1–441; UniProt 1–441 Author chain C; PDBConstruct 1–441; UniProt 1–441 Author chain D; PDBConstruct 1–441; UniProt 1–441 Author chain E; PDBConstruct 1–441; UniProt 1–441 Author chain G; PDBConstruct 1–441; UniProt 1–441

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 7qkh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7qkh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7qkh
Deposition date deposition_date2021-12-17
Structure title titleIn vitro assembled 258-391 tau filaments with sodium azide, (41a)
Keywords keywords;Alzheimer's Disease, Amyloid, Tau, Neurodegeneration, PROTEIN FIBRIL ;; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier28.45
Radius of gyration Rg (electron density) rg_electron32.17
Forward intensity I(0) i08050760.00
Molecular weight molecular_weight21586.0 kDa
Excluded volume excluded_volume27199 ų
Envelope volume envelope_volume36540 ų
Hydration-shell volume shell_volume12887 ų
Envelope diameter envelope_diameter129.9
Shell Rg shell_rg28.90
Envelope Rg envelope_rg33.51
Shape Rg shape_rg32.12
Total Rg total_rg31.97
Total atoms total_atoms3105
Residues n_residues204
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 dmax120.1
Rg (real space) rg_real29.71
Rg uncertainty (real space) rg_real_error2.55
I(0) (real space) i0_real8.0510e+06
I(0) uncertainty (real space) i0_real_error1.6670e+05
Rg (reciprocal space) rg_reciprocal29.31
I(0) (reciprocal space) i0_reciprocal8048000.0000
Solution quality estimate total_estimate0.6236
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary17.2
Skewness Skewness skewness0.841
Kurtosis Kurtosis kurtosis0.127
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha341700.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.046; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.001; Smooth: 0.963

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)