9m5k

The cryo-EM structure of in situ amplified (ISA) alpha-synuclein fibrils from PD homogenate

Method: ELECTRON MICROSCOPY Dmax: 72.4 Å Quality: REASONABLE

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

Alpha-synuclein

Homo sapiens

UniProt P37840

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 1–140 Chain B; UniProt 1–140 Chain C; UniProt 1–140 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

226 other PDB entries and 234 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SYUA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–140; UniProt 1–140 Author chain B; PDBConstruct 1–140; UniProt 1–140 Author chain C; PDBConstruct 1–140; UniProt 1–140

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 9m5k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9m5k
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9m5k
Deposition date deposition_date2025-03-06
Structure title titleThe cryo-EM structure of in situ amplified (ISA) alpha-synuclein fibrils from PD homogenate
Keywords keywordsamyloid, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier22.12
Radius of gyration Rg (electron density) rg_electron21.72
Forward intensity I(0) i011496000.00
Molecular weight molecular_weight25574.0 kDa
Excluded volume excluded_volume32307 ų
Envelope volume envelope_volume40315 ų
Hydration-shell volume shell_volume16473 ų
Envelope diameter envelope_diameter73.3
Shell Rg shell_rg27.00
Envelope Rg envelope_rg22.09
Shape Rg shape_rg21.70
Total Rg total_rg22.58
Total atoms total_atoms1797
Residues n_residues261
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 dmax72.4
Rg (real space) rg_real22.15
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real1.1500e+07
I(0) uncertainty (real space) i0_real_error1.7240e+05
Rg (reciprocal space) rg_reciprocal22.14
I(0) (reciprocal space) i0_reciprocal11500000.0000
Solution quality estimate total_estimate0.7280
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.275
Kurtosis Kurtosis kurtosis-0.572
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1493000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.939; Stabil: 1.000; Sysdev: 0.262; Positv: 1.000; Valcen: 0.881; Smooth: 0.975

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)