9gg1

P301T type I tau filaments from human brain

Method: ELECTRON MICROSCOPY Dmax: 99.4 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Isoform Tau-D of 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 215–321 Chain B; UniProt 215–321 Chain C; UniProt 215–321 Chain D; UniProt 215–321 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.26 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 1–107; UniProt 215–321 Author chain B; PDBConstruct 1–107; UniProt 215–321 Author chain C; PDBConstruct 1–107; UniProt 215–321 Author chain D; PDBConstruct 1–107; UniProt 215–321

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 9gg1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9gg1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9gg1
Deposition date deposition_date2024-08-12
最后修订 last_revision2024-09-11
Structure title titleP301T type I tau filaments from human brain
Keywords keywordsP301T tau, Frontotemporal dementia and parkinsonism linked to chromosome 17, Electron cryo-microscopy, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.56
Radius of gyration Rg (electron density) rg_electron31.93
Forward intensity I(0) i034644100.00
Molecular weight molecular_weight46037.0 kDa
Excluded volume excluded_volume57800 ų
Envelope volume envelope_volume75167 ų
Hydration-shell volume shell_volume21452 ų
Envelope diameter envelope_diameter107.6
Shell Rg shell_rg35.31
Envelope Rg envelope_rg32.12
Shape Rg shape_rg31.91
Total Rg total_rg32.30
Total atoms total_atoms3232
Residues n_residues428
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 dmax99.4
Rg (real space) rg_real31.85
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real3.4640e+07
I(0) uncertainty (real space) i0_real_error5.5990e+05
Rg (reciprocal space) rg_reciprocal31.73
I(0) (reciprocal space) i0_reciprocal34640000.0000
Solution quality estimate total_estimate0.7978
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary19.9
Skewness Skewness skewness0.362
Kurtosis Kurtosis kurtosis-0.637
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1448000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.667; Smooth: 0.108

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)