6qjm

Cryo-EM structure of heparin-induced 2N4R tau twister filaments

Method: ELECTRON MICROSCOPY Dmax: 59.3 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 274–321 Chain B; UniProt 274–321 Chain C; UniProt 274–321 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;20 mM Tris, pH 7.4, 100mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE;Blot force: -12 ; Blot time: 4s Resolution 3.30 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 1–48; UniProt 274–321 Author chain B; PDBConstruct 1–48; UniProt 274–321 Author chain C; PDBConstruct 1–48; UniProt 274–321

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 6qjm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6qjm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6qjm
Deposition date deposition_date2019-01-24
Structure title titleCryo-EM structure of heparin-induced 2N4R tau twister filaments
Keywords keywordsRecombinant tau protein, heparin, filament, cross-beta structure, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier17.44
Radius of gyration Rg (electron density) rg_electron17.00
Forward intensity I(0) i02690200.00
Molecular weight molecular_weight12102.0 kDa
Excluded volume excluded_volume15572 ų
Envelope volume envelope_volume20090 ų
Hydration-shell volume shell_volume10881 ų
Envelope diameter envelope_diameter58.1
Shell Rg shell_rg21.41
Envelope Rg envelope_rg17.35
Shape Rg shape_rg16.94
Total Rg total_rg18.16
Total atoms total_atoms846
Residues n_residues111
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 dmax59.3
Rg (real space) rg_real17.51
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real2.6900e+06
I(0) uncertainty (real space) i0_real_error3.2150e+04
Rg (reciprocal space) rg_reciprocal17.51
I(0) (reciprocal space) i0_reciprocal2690000.0000
Solution quality estimate total_estimate0.7850
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.8
Skewness Skewness skewness0.325
Kurtosis Kurtosis kurtosis-0.590
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha492300.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.829; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.716; 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)