9czl

Straight tau filaments in dominantly inherited Alzheimer disease with cotton wool plaques

Method: ELECTRON MICROSCOPY Dmax: 129.6 Å Quality: REASONABLE

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

Isoform Tau-C 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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 274–347 Chain B; UniProt 274–347 Chain C; UniProt 274–347 Chain D; UniProt 274–347 Chain E; UniProt 274–347 Chain F; UniProt 274–347 Chain G; UniProt 274–347 Chain H; UniProt 274–347 Chain I; UniProt 274–347 Chain J; UniProt 274–347 Fragment:UNP residues 274-347 No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 P10636-5
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–74; UniProt 274–347 Author chain B; PDBConstruct 1–74; UniProt 274–347 Author chain C; PDBConstruct 1–74; UniProt 274–347 Author chain D; PDBConstruct 1–74; UniProt 274–347 Author chain E; PDBConstruct 1–74; UniProt 274–347 Author chain F; PDBConstruct 1–74; UniProt 274–347 Author chain G; PDBConstruct 1–74; UniProt 274–347 Author chain H; PDBConstruct 1–74; UniProt 274–347 Author chain I; PDBConstruct 1–74; UniProt 274–347 Author chain J; PDBConstruct 1–74; UniProt 274–347

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 9czl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9czl
Deposition date deposition_date2024-08-05
最后修订 last_revision2024-10-02
Structure title titleStraight tau filaments in dominantly inherited Alzheimer disease with cotton wool plaques
Keywords keywordsTau filaments, SF, cotton wool plaques, neurodegeneration, NEUROPEPTIDE, PROTEIN FIBRIL; NEUROPEPTIDE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.34
Radius of gyration Rg (electron density) rg_electron36.75
Forward intensity I(0) i097766100.00
Molecular weight molecular_weight80414.0 kDa
Excluded volume excluded_volume101630 ų
Envelope volume envelope_volume137980 ų
Hydration-shell volume shell_volume34024 ų
Envelope diameter envelope_diameter128.0
Shell Rg shell_rg39.08
Envelope Rg envelope_rg36.66
Shape Rg shape_rg36.76
Total Rg total_rg36.88
Total atoms total_atoms5660
Residues n_residues740
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 dmax129.6
Rg (real space) rg_real36.69
Rg uncertainty (real space) rg_real_error1.45
I(0) (real space) i0_real9.7770e+07
I(0) uncertainty (real space) i0_real_error1.6450e+06
Rg (reciprocal space) rg_reciprocal36.47
I(0) (reciprocal space) i0_reciprocal97750000.0000
Solution quality estimate total_estimate0.6279
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.3
Skewness Skewness skewness0.518
Kurtosis Kurtosis kurtosis-0.284
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3964000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.753; Stabil: 1.000; Sysdev: 0.101; Positv: 1.000; Valcen: 0.714; Smooth: 0.882

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)