4znn

MicroED structure of the segment, GVVHGVTTVA, from the A53T familial mutant of Parkinson's disease protein, alpha-synuclein residues 47-56

Method: ELECTRON CRYSTALLOGRAPHY Dmax: 35.9 Å Quality: REASONABLE

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

Alpha-synuclein

OrganismNot specified

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 47–56 Mutation:A53T No other associated polymer ELECTRON CRYSTALLOGRAPHY X-ray crystallization conditions:BATCH MODE;pH 7;310 K;1 mg of synthetic peptide GVVHGVTTVA was dissolved in 200 microliters of 50 mM phosphate buffer pH 7.0 and 0.1% w/v DMSO and shaken overnight in an orbital mixing plate Resolution 1.41 Å R-free 0.282

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 1–10; UniProt 47–56

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 4znn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4znn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4znn
Deposition date deposition_date2015-05-05
Structure title titleMicroED structure of the segment, GVVHGVTTVA, from the A53T familial mutant of Parkinson's disease protein, alpha-synuclein residues 47-56
Keywords keywords;Amyloid, alpha-synuclein, Parkinson's Disease, Toxic Core, NACore, LIPID BINDING PROTEIN ;; LIPID BINDING PROTEIN
Experimental Method methodELECTRON CRYSTALLOGRAPHY

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

Radius of gyration Rg (Guinier) rg_guinier9.64
Radius of gyration Rg (electron density) rg_electron8.77
Forward intensity I(0) i039512.90
Molecular weight molecular_weight939.1 kDa
Excluded volume excluded_volume1186 ų
Envelope volume envelope_volume1582 ų
Hydration-shell volume shell_volume2173 ų
Envelope diameter envelope_diameter31.8
Shell Rg shell_rg11.50
Envelope Rg envelope_rg9.39
Shape Rg shape_rg8.71
Total Rg total_rg10.20
Total atoms total_atoms66
Residues n_residues10
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 dmax35.9
Rg (real space) rg_real9.86
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real3.9510e+04
I(0) uncertainty (real space) i0_real_error4.7200e+02
Rg (reciprocal space) rg_reciprocal9.85
I(0) (reciprocal space) i0_reciprocal39510.0000
Solution quality estimate total_estimate0.7494
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary8.6
Skewness Skewness skewness0.600
Kurtosis Kurtosis kurtosis-0.202
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3024.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.585; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.138; Smooth: 0.844

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)