8p34

Tau filaments extracted from human brain with the DeltaK281 mutation in MAPT

Method: ELECTRON MICROSCOPY Dmax: 120.0 Å Quality: REASONABLE

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 196–289 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;20 mM Tris-HCL, 100 mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.61 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 P10636-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–94; UniProt 196–289

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 8p34

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8p34
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8p34
Deposition date deposition_date2023-05-17
Structure title titleTau filaments extracted from human brain with the DeltaK281 mutation in MAPT
Keywords keywordsDeltaK281, Tau, Amyloid filament, Cross-beta-sheet, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.20
Radius of gyration Rg (electron density) rg_electron33.39
Forward intensity I(0) i01907470.00
Molecular weight molecular_weight10106.0 kDa
Excluded volume excluded_volume12719 ų
Envelope volume envelope_volume22761 ų
Hydration-shell volume shell_volume7318 ų
Envelope diameter envelope_diameter117.9
Shell Rg shell_rg30.28
Envelope Rg envelope_rg32.97
Shape Rg shape_rg33.33
Total Rg total_rg33.14
Total atoms total_atoms711
Residues n_residues94
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 dmax120.0
Rg (real space) rg_real33.10
Rg uncertainty (real space) rg_real_error1.44
I(0) (real space) i0_real1.9070e+06
I(0) uncertainty (real space) i0_real_error3.2280e+04
Rg (reciprocal space) rg_reciprocal32.72
I(0) (reciprocal space) i0_reciprocal1907000.0000
Solution quality estimate total_estimate0.6789
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary19.6
Skewness Skewness skewness0.582
Kurtosis Kurtosis kurtosis-0.477
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha239800.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.305; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.065; Smooth: 0.840

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)