8v1n

Cryo-EM structure of tau filaments made from jR2R3-P301L peptides induced with heparin

Method: ELECTRON MICROSCOPY Dmax: 64.0 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: dodecameric(12) Consistent with protein copy count Chain A; UniProt 612–630 Chain B; UniProt 612–630 Chain C; UniProt 612–630 Chain D; UniProt 612–630 Chain E; UniProt 612–630 Chain F; UniProt 612–630 Chain G; UniProt 612–630 Chain H; UniProt 612–630 Chain I; UniProt 612–630 Chain J; UniProt 612–630 Chain K; UniProt 612–630 Chain L; UniProt 612–630 Mutation:P618L No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;20mM ammoniium acetate, 50mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 1–19; UniProt 612–630 Author chain B; PDBConstruct 1–19; UniProt 612–630 Author chain C; PDBConstruct 1–19; UniProt 612–630 Author chain D; PDBConstruct 1–19; UniProt 612–630 Author chain E; PDBConstruct 1–19; UniProt 612–630 Author chain F; PDBConstruct 1–19; UniProt 612–630 Author chain G; PDBConstruct 1–19; UniProt 612–630 Author chain H; PDBConstruct 1–19; UniProt 612–630 Author chain I; PDBConstruct 1–19; UniProt 612–630 Author chain J; PDBConstruct 1–19; UniProt 612–630 Author chain K; PDBConstruct 1–19; UniProt 612–630 Author chain L; PDBConstruct 1–19; UniProt 612–630

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 8v1n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8v1n
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8v1n
Deposition date deposition_date2023-11-20
Structure title titleCryo-EM structure of tau filaments made from jR2R3-P301L peptides induced with heparin
Keywords keywordstau, amyloid, filament, P301L, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier19.00
Radius of gyration Rg (electron density) rg_electron18.84
Forward intensity I(0) i06473660.00
Molecular weight molecular_weight20364.0 kDa
Excluded volume excluded_volume26330 ų
Envelope volume envelope_volume31089 ų
Hydration-shell volume shell_volume14418 ų
Envelope diameter envelope_diameter64.9
Shell Rg shell_rg24.24
Envelope Rg envelope_rg19.30
Shape Rg shape_rg18.84
Total Rg total_rg19.77
Total atoms total_atoms1440
Residues n_residues192
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 dmax64.0
Rg (real space) rg_real19.10
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real6.4740e+06
I(0) uncertainty (real space) i0_real_error8.2990e+04
Rg (reciprocal space) rg_reciprocal19.09
I(0) (reciprocal space) i0_reciprocal6474000.0000
Solution quality estimate total_estimate0.7894
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.7
Skewness Skewness skewness0.469
Kurtosis Kurtosis kurtosis-0.223
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1685000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.802; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.855; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)