7ql1

In vitro assembled 266-391 tau filaments in PBS (23a)

Method: ELECTRON MICROSCOPY Dmax: 84.5 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–441 Chain C; UniProt 1–441 Chain D; UniProt 1–441 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.34 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 C; PDBConstruct 1–441; UniProt 1–441 Author chain D; 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 7ql1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ql1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ql1
Deposition date deposition_date2021-12-19
Structure title titleIn vitro assembled 266-391 tau filaments in PBS (23a)
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_guinier25.82
Radius of gyration Rg (electron density) rg_electron26.03
Forward intensity I(0) i09446400.00
Molecular weight molecular_weight23737.0 kDa
Excluded volume excluded_volume29954 ų
Envelope volume envelope_volume40727 ų
Hydration-shell volume shell_volume13784 ų
Envelope diameter envelope_diameter86.8
Shell Rg shell_rg31.55
Envelope Rg envelope_rg25.65
Shape Rg shape_rg25.99
Total Rg total_rg26.82
Total atoms total_atoms1671
Residues n_residues219
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 dmax84.5
Rg (real space) rg_real25.98
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real9.4460e+06
I(0) uncertainty (real space) i0_real_error1.3740e+05
Rg (reciprocal space) rg_reciprocal25.94
I(0) (reciprocal space) i0_reciprocal9446000.0000
Solution quality estimate total_estimate0.8240
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.6
Skewness Skewness skewness0.264
Kurtosis Kurtosis kurtosis-0.834
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha461800.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.767; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.516; Smooth: 0.890

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)