8ttn

PHF1-Phosphomimetic Tau Filaments (Full-length, Cofactor-Free 0N4R Tau S396E, S400E, T403E, S404E)

Method: ELECTRON MICROSCOPY Dmax: 97.7 Å Quality: GOOD

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–383 Chain B; UniProt 1–383 Chain C; UniProt 1–383 Chain D; UniProt 1–383 Chain E; UniProt 1–383 Mutation:S396E, S400E, T403E, S404E No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8;50 mM K2HPO4 buffer, pH 6.8, containing 300 mM NaCl, 5 mM DTT, and 1x cOmplete protease inhibitor cocktail tablet (Roche) per 40 ml fibrillization buffer. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.40 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 1–383; UniProt 1–383 Author chain B; PDBConstruct 1–383; UniProt 1–383 Author chain C; PDBConstruct 1–383; UniProt 1–383 Author chain D; PDBConstruct 1–383; UniProt 1–383 Author chain E; PDBConstruct 1–383; UniProt 1–383

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 8ttn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ttn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ttn
Deposition date deposition_date2023-08-14
最后修订 last_revision2024-06-26
Structure title titlePHF1-Phosphomimetic Tau Filaments (Full-length, Cofactor-Free 0N4R Tau S396E, S400E, T403E, S404E)
Keywords keywordsTau, Amyloid Fibril, Phosphomimetic, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier28.02
Radius of gyration Rg (electron density) rg_electron27.96
Forward intensity I(0) i039315900.00
Molecular weight molecular_weight48191.0 kDa
Excluded volume excluded_volume60422 ų
Envelope volume envelope_volume76102 ų
Hydration-shell volume shell_volume24925 ų
Envelope diameter envelope_diameter101.3
Shell Rg shell_rg32.57
Envelope Rg envelope_rg28.21
Shape Rg shape_rg28.03
Total Rg total_rg28.24
Total atoms total_atoms6919
Residues n_residues450
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 dmax97.7
Rg (real space) rg_real28.48
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real3.9320e+07
I(0) uncertainty (real space) i0_real_error5.6300e+05
Rg (reciprocal space) rg_reciprocal28.34
I(0) (reciprocal space) i0_reciprocal39310000.0000
Solution quality estimate total_estimate0.7949
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.7
Skewness Skewness skewness0.647
Kurtosis Kurtosis kurtosis-0.202
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7953000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.627; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.595; Smooth: 0.854

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)