8p94

Cryo-EM structure of cortactin stabilized Arp2/3-complex nucleated actin branches

Method: ELECTRON MICROSCOPY Dmax: 230.1 Å Quality: EXCELLENT

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

Actin-related protein 3

Homo sapiens

UniProt P61158

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 heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain A; UniProt 1–418 Not recorded Actin-related protein 2 × 1 (P61160) Actin-related protein 2/3 complex subunit 1B × 1 (O15143) Actin-related protein 2/3 complex subunit 2 × 1 (O15144) Actin-related protein 2/3 complex subunit 3 × 1 (O15145) Actin-related protein 2/3 complex subunit 4 × 1 (P59998) Actin-related protein 2/3 complex subunit 5-like protein × 1 (Q9BPX5) Actin, cytoplasmic 1 × 10 (Q6QAQ1) Src substrate cortactin × 1 (Q60598) F-actin-capping protein subunit alpha-1 × 1 (P47753) Isoform 2 of F-actin-capping protein subunit beta × 1 (P47757) Phalloidin × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 50mM KCl, 1mM EGTA, 1mM MgCl2, 0.2 mM ATP and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;Back blotting 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARP3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–418; UniProt 1–418

Actin-related protein 2

Homo sapiens

UniProt P61160

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 heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain B; UniProt 1–394 Not recorded Actin-related protein 3 × 1 (P61158) Actin-related protein 2/3 complex subunit 1B × 1 (O15143) Actin-related protein 2/3 complex subunit 2 × 1 (O15144) Actin-related protein 2/3 complex subunit 3 × 1 (O15145) Actin-related protein 2/3 complex subunit 4 × 1 (P59998) Actin-related protein 2/3 complex subunit 5-like protein × 1 (Q9BPX5) Actin, cytoplasmic 1 × 10 (Q6QAQ1) Src substrate cortactin × 1 (Q60598) F-actin-capping protein subunit alpha-1 × 1 (P47753) Isoform 2 of F-actin-capping protein subunit beta × 1 (P47757) Phalloidin × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 50mM KCl, 1mM EGTA, 1mM MgCl2, 0.2 mM ATP and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;Back blotting 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARP2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–394; UniProt 1–394

Actin-related protein 2/3 complex subunit 1B

Homo sapiens

UniProt O15143

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 heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain C; UniProt 1–372 Not recorded Actin-related protein 3 × 1 (P61158) Actin-related protein 2 × 1 (P61160) Actin-related protein 2/3 complex subunit 2 × 1 (O15144) Actin-related protein 2/3 complex subunit 3 × 1 (O15145) Actin-related protein 2/3 complex subunit 4 × 1 (P59998) Actin-related protein 2/3 complex subunit 5-like protein × 1 (Q9BPX5) Actin, cytoplasmic 1 × 10 (Q6QAQ1) Src substrate cortactin × 1 (Q60598) F-actin-capping protein subunit alpha-1 × 1 (P47753) Isoform 2 of F-actin-capping protein subunit beta × 1 (P47757) Phalloidin × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 50mM KCl, 1mM EGTA, 1mM MgCl2, 0.2 mM ATP and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;Back blotting 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARC1B_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–372; UniProt 1–372

Actin-related protein 2/3 complex subunit 2

Homo sapiens

UniProt O15144

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 heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain D; UniProt 1–300 Not recorded Actin-related protein 3 × 1 (P61158) Actin-related protein 2 × 1 (P61160) Actin-related protein 2/3 complex subunit 1B × 1 (O15143) Actin-related protein 2/3 complex subunit 3 × 1 (O15145) Actin-related protein 2/3 complex subunit 4 × 1 (P59998) Actin-related protein 2/3 complex subunit 5-like protein × 1 (Q9BPX5) Actin, cytoplasmic 1 × 10 (Q6QAQ1) Src substrate cortactin × 1 (Q60598) F-actin-capping protein subunit alpha-1 × 1 (P47753) Isoform 2 of F-actin-capping protein subunit beta × 1 (P47757) Phalloidin × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 50mM KCl, 1mM EGTA, 1mM MgCl2, 0.2 mM ATP and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;Back blotting 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC2_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–300; UniProt 1–300

Actin-related protein 2/3 complex subunit 3

Homo sapiens

UniProt O15145

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 heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain E; UniProt 1–178 Not recorded Actin-related protein 3 × 1 (P61158) Actin-related protein 2 × 1 (P61160) Actin-related protein 2/3 complex subunit 1B × 1 (O15143) Actin-related protein 2/3 complex subunit 2 × 1 (O15144) Actin-related protein 2/3 complex subunit 4 × 1 (P59998) Actin-related protein 2/3 complex subunit 5-like protein × 1 (Q9BPX5) Actin, cytoplasmic 1 × 10 (Q6QAQ1) Src substrate cortactin × 1 (Q60598) F-actin-capping protein subunit alpha-1 × 1 (P47753) Isoform 2 of F-actin-capping protein subunit beta × 1 (P47757) Phalloidin × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 50mM KCl, 1mM EGTA, 1mM MgCl2, 0.2 mM ATP and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;Back blotting 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC3_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–178; UniProt 1–178

Actin-related protein 2/3 complex subunit 4

Homo sapiens

UniProt P59998

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 heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain F; UniProt 1–168 Not recorded Actin-related protein 3 × 1 (P61158) Actin-related protein 2 × 1 (P61160) Actin-related protein 2/3 complex subunit 1B × 1 (O15143) Actin-related protein 2/3 complex subunit 2 × 1 (O15144) Actin-related protein 2/3 complex subunit 3 × 1 (O15145) Actin-related protein 2/3 complex subunit 5-like protein × 1 (Q9BPX5) Actin, cytoplasmic 1 × 10 (Q6QAQ1) Src substrate cortactin × 1 (Q60598) F-actin-capping protein subunit alpha-1 × 1 (P47753) Isoform 2 of F-actin-capping protein subunit beta × 1 (P47757) Phalloidin × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 50mM KCl, 1mM EGTA, 1mM MgCl2, 0.2 mM ATP and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;Back blotting 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC4_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–168; UniProt 1–168

Actin-related protein 2/3 complex subunit 5-like protein

Homo sapiens

UniProt Q9BPX5

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 heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain G; UniProt 1–153 Not recorded Actin-related protein 3 × 1 (P61158) Actin-related protein 2 × 1 (P61160) Actin-related protein 2/3 complex subunit 1B × 1 (O15143) Actin-related protein 2/3 complex subunit 2 × 1 (O15144) Actin-related protein 2/3 complex subunit 3 × 1 (O15145) Actin-related protein 2/3 complex subunit 4 × 1 (P59998) Actin, cytoplasmic 1 × 10 (Q6QAQ1) Src substrate cortactin × 1 (Q60598) F-actin-capping protein subunit alpha-1 × 1 (P47753) Isoform 2 of F-actin-capping protein subunit beta × 1 (P47757) Phalloidin × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 50mM KCl, 1mM EGTA, 1mM MgCl2, 0.2 mM ATP and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;Back blotting 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARP5L_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–153; UniProt 1–153

Actin, cytoplasmic 1

OrganismNot specified

UniProt Q6QAQ1

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 heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain H; UniProt 1–375 Chain J; UniProt 1–375 Chain K; UniProt 1–375 Chain N; UniProt 1–375 Chain O; UniProt 1–375 Chain P; UniProt 1–375 Chain Q; UniProt 1–375 Chain R; UniProt 1–375 Chain S; UniProt 1–375 Chain W; UniProt 1–375 Not recorded Actin-related protein 3 × 1 (P61158) Actin-related protein 2 × 1 (P61160) Actin-related protein 2/3 complex subunit 1B × 1 (O15143) Actin-related protein 2/3 complex subunit 2 × 1 (O15144) Actin-related protein 2/3 complex subunit 3 × 1 (O15145) Actin-related protein 2/3 complex subunit 4 × 1 (P59998) Actin-related protein 2/3 complex subunit 5-like protein × 1 (Q9BPX5) Src substrate cortactin × 1 (Q60598) F-actin-capping protein subunit alpha-1 × 1 (P47753) Isoform 2 of F-actin-capping protein subunit beta × 1 (P47757) Phalloidin × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 50mM KCl, 1mM EGTA, 1mM MgCl2, 0.2 mM ATP and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;Back blotting 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.

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTB_PIG
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–375; UniProt 1–375 Author chain J; PDBConstruct 1–375; UniProt 1–375 Author chain K; PDBConstruct 1–375; UniProt 1–375 Author chain N; PDBConstruct 1–375; UniProt 1–375 Author chain O; PDBConstruct 1–375; UniProt 1–375 Author chain P; PDBConstruct 1–375; UniProt 1–375 Author chain Q; PDBConstruct 1–375; UniProt 1–375 Author chain R; PDBConstruct 1–375; UniProt 1–375 Author chain S; PDBConstruct 1–375; UniProt 1–375 Author chain W; PDBConstruct 1–375; UniProt 1–375

Src substrate cortactin

Mus musculus

UniProt Q60598

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 heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain I; UniProt 1–546 Not recorded Actin-related protein 3 × 1 (P61158) Actin-related protein 2 × 1 (P61160) Actin-related protein 2/3 complex subunit 1B × 1 (O15143) Actin-related protein 2/3 complex subunit 2 × 1 (O15144) Actin-related protein 2/3 complex subunit 3 × 1 (O15145) Actin-related protein 2/3 complex subunit 4 × 1 (P59998) Actin-related protein 2/3 complex subunit 5-like protein × 1 (Q9BPX5) Actin, cytoplasmic 1 × 10 (Q6QAQ1) F-actin-capping protein subunit alpha-1 × 1 (P47753) Isoform 2 of F-actin-capping protein subunit beta × 1 (P47757) Phalloidin × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 50mM KCl, 1mM EGTA, 1mM MgCl2, 0.2 mM ATP and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;Back blotting 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.

6 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SRC8_MOUSE
Isoform
PDB entities 9
Chains and sequence ranges Author chain I; PDBConstruct 1–546; UniProt 1–546

F-actin-capping protein subunit alpha-1

Mus musculus

UniProt P47753

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 heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain U; UniProt 1–286 Not recorded Actin-related protein 3 × 1 (P61158) Actin-related protein 2 × 1 (P61160) Actin-related protein 2/3 complex subunit 1B × 1 (O15143) Actin-related protein 2/3 complex subunit 2 × 1 (O15144) Actin-related protein 2/3 complex subunit 3 × 1 (O15145) Actin-related protein 2/3 complex subunit 4 × 1 (P59998) Actin-related protein 2/3 complex subunit 5-like protein × 1 (Q9BPX5) Actin, cytoplasmic 1 × 10 (Q6QAQ1) Src substrate cortactin × 1 (Q60598) Isoform 2 of F-actin-capping protein subunit beta × 1 (P47757) Phalloidin × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 50mM KCl, 1mM EGTA, 1mM MgCl2, 0.2 mM ATP and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;Back blotting 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAZA1_MOUSE
Isoform
PDB entities 10
Chains and sequence ranges Author chain U; PDBConstruct 1–286; UniProt 1–286

Isoform 2 of F-actin-capping protein subunit beta

Mus musculus

UniProt P47757

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 heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain V; UniProt 1–272 Not recorded Actin-related protein 3 × 1 (P61158) Actin-related protein 2 × 1 (P61160) Actin-related protein 2/3 complex subunit 1B × 1 (O15143) Actin-related protein 2/3 complex subunit 2 × 1 (O15144) Actin-related protein 2/3 complex subunit 3 × 1 (O15145) Actin-related protein 2/3 complex subunit 4 × 1 (P59998) Actin-related protein 2/3 complex subunit 5-like protein × 1 (Q9BPX5) Actin, cytoplasmic 1 × 10 (Q6QAQ1) Src substrate cortactin × 1 (Q60598) F-actin-capping protein subunit alpha-1 × 1 (P47753) Phalloidin × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 50mM KCl, 1mM EGTA, 1mM MgCl2, 0.2 mM ATP and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;Back blotting 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAPZB_MOUSE
Isoform P47757-2
PDB entities 11
Chains and sequence ranges Author chain V; PDBConstruct 1–272; UniProt 1–272

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 8p94

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8p94
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8p94
Deposition date deposition_date2023-06-05
Structure title titleCryo-EM structure of cortactin stabilized Arp2/3-complex nucleated actin branches
Keywords keywordsComplex, CONTRACTILE PROTEIN; CONTRACTILE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier82.08
Radius of gyration Rg (electron density) rg_electron83.20
Forward intensity I(0) i07348910000.00
Molecular weight molecular_weight721940.0 kDa
Excluded volume excluded_volume901270 ų
Envelope volume envelope_volume1338900 ų
Hydration-shell volume shell_volume146080 ų
Envelope diameter envelope_diameter305.1
Shell Rg shell_rg67.66
Envelope Rg envelope_rg84.85
Shape Rg shape_rg83.22
Total Rg total_rg82.94
Total atoms total_atoms100470
Residues n_residues6370
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 dmax230.1
Rg (real space) rg_real77.36
Rg uncertainty (real space) rg_real_error1.25
I(0) (real space) i0_real7.0910e+09
I(0) uncertainty (real space) i0_real_error1.4120e+08
Rg (reciprocal space) rg_reciprocal78.16
I(0) (reciprocal space) i0_reciprocal7269000000.0000
Solution quality estimate total_estimate0.9076
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary72.7
Skewness Skewness skewness0.485
Kurtosis Kurtosis kurtosis-0.478
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha0.2729
Highest regularization parameter α highest_alpha291200000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.939; Stabil: 0.985; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.059

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

8. Citations (1)

9. Files and Curves (10)