7qk5

In vitro assembled 266/297 - 391 tau filaments with KCl (10a)

Method: ELECTRON MICROSCOPY Dmax: 139.1 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 × 9 PDB declaration: nonameric(9) 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 F; UniProt 1–441 Chain G; UniProt 1–441 Chain H; UniProt 1–441 Chain K; UniProt 1–441 Not recorded CL CHLORIDE ION × 18 K POTASSIUM ION × 18 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 1.92 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 F; PDBConstruct 1–441; UniProt 1–441 Author chain G; PDBConstruct 1–441; UniProt 1–441 Author chain H; PDBConstruct 1–441; UniProt 1–441 Author chain K; 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 7qk5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7qk5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7qk5
Deposition date deposition_date2021-12-17
Structure title titleIn vitro assembled 266/297 - 391 tau filaments with KCl (10a)
Keywords keywords;Alzheimer's Disease, Amyloid, Tau, Neurodegeneration, chronic traumatic encephalopathy, PROTEIN FIBRIL ;; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.65
Radius of gyration Rg (electron density) rg_electron43.40
Forward intensity I(0) i078797400.00
Molecular weight molecular_weight73966.0 kDa
Excluded volume excluded_volume93491 ų
Envelope volume envelope_volume140290 ų
Hydration-shell volume shell_volume28786 ų
Envelope diameter envelope_diameter138.9
Shell Rg shell_rg43.77
Envelope Rg envelope_rg43.43
Shape Rg shape_rg43.47
Total Rg total_rg43.14
Total atoms total_atoms10485
Residues n_residues666
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 dmax139.1
Rg (real space) rg_real41.82
Rg uncertainty (real space) rg_real_error1.60
I(0) (real space) i0_real7.8800e+07
I(0) uncertainty (real space) i0_real_error1.3830e+06
Rg (reciprocal space) rg_reciprocal41.65
I(0) (reciprocal space) i0_reciprocal78780000.0000
Solution quality estimate total_estimate0.8625
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.6
Skewness Skewness skewness0.334
Kurtosis Kurtosis kurtosis-0.424
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2630000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.908; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.518

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)