9tgg

Cryo-EM structure of Spinacia oleracea cytochrome b6f complex with bound plastocyanin

Method: ELECTRON MICROSCOPY Dmax: 147.2 Å Quality: REASONABLE

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

Cytochrome b6

OrganismNot specified

UniProt P00165

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 × 17 PDB declaration: 17-meric(17) Consistent with protein copy count Chain A; UniProt 1–215 Chain I; UniProt 1–215 Not recorded Cytochrome b6-f complex subunit 4 × 2 (P00166) Cytochrome f × 2 (P16013) Cytochrome b6-f complex iron-sulfur subunit, chloroplastic × 2 (P08980) Cytochrome b6-f complex subunit 6 × 2 (Q9M3L0) Cytochrome b6-f complex subunit 7 × 2 (P80883) Cytochrome b6-f complex subunit 5 × 2 (P69461) Cytochrome b6-f complex subunit 8 × 2 (P61045) Plastocyanin, chloroplastic × 1 (P00289) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 4 UMQ UNDECYL-MALTOSIDE × 6 PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-BENZOQUINONE × 7 CLA CHLOROPHYLL A × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL × 2 BCR BETA-CAROTENE × 2 CU COPPER (II) ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYB6_SPIOL
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–215; UniProt 1–215 Author chain I; PDBConstruct 1–215; UniProt 1–215

Cytochrome b6-f complex subunit 4

OrganismNot specified

UniProt P00166

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 × 17 PDB declaration: 17-meric(17) Consistent with protein copy count Chain B; UniProt 1–160 Chain J; UniProt 1–160 Not recorded Cytochrome b6 × 2 (P00165) Cytochrome f × 2 (P16013) Cytochrome b6-f complex iron-sulfur subunit, chloroplastic × 2 (P08980) Cytochrome b6-f complex subunit 6 × 2 (Q9M3L0) Cytochrome b6-f complex subunit 7 × 2 (P80883) Cytochrome b6-f complex subunit 5 × 2 (P69461) Cytochrome b6-f complex subunit 8 × 2 (P61045) Plastocyanin, chloroplastic × 1 (P00289) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 4 UMQ UNDECYL-MALTOSIDE × 6 PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-BENZOQUINONE × 7 CLA CHLOROPHYLL A × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL × 2 BCR BETA-CAROTENE × 2 CU COPPER (II) ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PETD_SPIOL
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–160; UniProt 1–160 Author chain J; PDBConstruct 1–160; UniProt 1–160

Cytochrome f

OrganismNot specified

UniProt P16013

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 × 17 PDB declaration: 17-meric(17) Consistent with protein copy count Chain C; UniProt 36–320 Chain K; UniProt 36–320 Not recorded Cytochrome b6 × 2 (P00165) Cytochrome b6-f complex subunit 4 × 2 (P00166) Cytochrome b6-f complex iron-sulfur subunit, chloroplastic × 2 (P08980) Cytochrome b6-f complex subunit 6 × 2 (Q9M3L0) Cytochrome b6-f complex subunit 7 × 2 (P80883) Cytochrome b6-f complex subunit 5 × 2 (P69461) Cytochrome b6-f complex subunit 8 × 2 (P61045) Plastocyanin, chloroplastic × 1 (P00289) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 4 UMQ UNDECYL-MALTOSIDE × 6 PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-BENZOQUINONE × 7 CLA CHLOROPHYLL A × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL × 2 BCR BETA-CAROTENE × 2 CU COPPER (II) ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYF_SPIOL
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–285; UniProt 36–320 Author chain K; PDBConstruct 1–285; UniProt 36–320

Cytochrome b6-f complex iron-sulfur subunit, chloroplastic

OrganismNot specified

UniProt P08980

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 × 17 PDB declaration: 17-meric(17) Consistent with protein copy count Chain D; UniProt 52–230 Chain L; UniProt 52–230 Not recorded Cytochrome b6 × 2 (P00165) Cytochrome b6-f complex subunit 4 × 2 (P00166) Cytochrome f × 2 (P16013) Cytochrome b6-f complex subunit 6 × 2 (Q9M3L0) Cytochrome b6-f complex subunit 7 × 2 (P80883) Cytochrome b6-f complex subunit 5 × 2 (P69461) Cytochrome b6-f complex subunit 8 × 2 (P61045) Plastocyanin, chloroplastic × 1 (P00289) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 4 UMQ UNDECYL-MALTOSIDE × 6 PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-BENZOQUINONE × 7 CLA CHLOROPHYLL A × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL × 2 BCR BETA-CAROTENE × 2 CU COPPER (II) ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCRIA_SPIOL
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–179; UniProt 52–230 Author chain L; PDBConstruct 1–179; UniProt 52–230

Cytochrome b6-f complex subunit 6

OrganismNot specified

UniProt Q9M3L0

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 × 17 PDB declaration: 17-meric(17) Consistent with protein copy count Chain E; UniProt 1–31 Chain M; UniProt 1–31 Not recorded Cytochrome b6 × 2 (P00165) Cytochrome b6-f complex subunit 4 × 2 (P00166) Cytochrome f × 2 (P16013) Cytochrome b6-f complex iron-sulfur subunit, chloroplastic × 2 (P08980) Cytochrome b6-f complex subunit 7 × 2 (P80883) Cytochrome b6-f complex subunit 5 × 2 (P69461) Cytochrome b6-f complex subunit 8 × 2 (P61045) Plastocyanin, chloroplastic × 1 (P00289) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 4 UMQ UNDECYL-MALTOSIDE × 6 PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-BENZOQUINONE × 7 CLA CHLOROPHYLL A × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL × 2 BCR BETA-CAROTENE × 2 CU COPPER (II) ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PETL_SPIOL
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–31; UniProt 1–31 Author chain M; PDBConstruct 1–31; UniProt 1–31

Cytochrome b6-f complex subunit 7

OrganismNot specified

UniProt P80883

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 × 17 PDB declaration: 17-meric(17) Consistent with protein copy count Chain F; UniProt 1–36 Chain N; UniProt 1–36 Not recorded Cytochrome b6 × 2 (P00165) Cytochrome b6-f complex subunit 4 × 2 (P00166) Cytochrome f × 2 (P16013) Cytochrome b6-f complex iron-sulfur subunit, chloroplastic × 2 (P08980) Cytochrome b6-f complex subunit 6 × 2 (Q9M3L0) Cytochrome b6-f complex subunit 5 × 2 (P69461) Cytochrome b6-f complex subunit 8 × 2 (P61045) Plastocyanin, chloroplastic × 1 (P00289) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 4 UMQ UNDECYL-MALTOSIDE × 6 PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-BENZOQUINONE × 7 CLA CHLOROPHYLL A × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL × 2 BCR BETA-CAROTENE × 2 CU COPPER (II) ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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 PETM_SPIOL
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–36; UniProt 1–36 Author chain N; PDBConstruct 1–36; UniProt 1–36

Cytochrome b6-f complex subunit 5

OrganismNot specified

UniProt P69461

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 × 17 PDB declaration: 17-meric(17) Consistent with protein copy count Chain G; UniProt 1–37 Chain O; UniProt 1–37 Not recorded Cytochrome b6 × 2 (P00165) Cytochrome b6-f complex subunit 4 × 2 (P00166) Cytochrome f × 2 (P16013) Cytochrome b6-f complex iron-sulfur subunit, chloroplastic × 2 (P08980) Cytochrome b6-f complex subunit 6 × 2 (Q9M3L0) Cytochrome b6-f complex subunit 7 × 2 (P80883) Cytochrome b6-f complex subunit 8 × 2 (P61045) Plastocyanin, chloroplastic × 1 (P00289) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 4 UMQ UNDECYL-MALTOSIDE × 6 PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-BENZOQUINONE × 7 CLA CHLOROPHYLL A × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL × 2 BCR BETA-CAROTENE × 2 CU COPPER (II) ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PETG_SPIOL
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–37; UniProt 1–37 Author chain O; PDBConstruct 1–37; UniProt 1–37

Cytochrome b6-f complex subunit 8

OrganismNot specified

UniProt P61045

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 × 17 PDB declaration: 17-meric(17) Consistent with protein copy count Chain H; UniProt 1–29 Chain P; UniProt 1–29 Not recorded Cytochrome b6 × 2 (P00165) Cytochrome b6-f complex subunit 4 × 2 (P00166) Cytochrome f × 2 (P16013) Cytochrome b6-f complex iron-sulfur subunit, chloroplastic × 2 (P08980) Cytochrome b6-f complex subunit 6 × 2 (Q9M3L0) Cytochrome b6-f complex subunit 7 × 2 (P80883) Cytochrome b6-f complex subunit 5 × 2 (P69461) Plastocyanin, chloroplastic × 1 (P00289) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 4 UMQ UNDECYL-MALTOSIDE × 6 PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-BENZOQUINONE × 7 CLA CHLOROPHYLL A × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL × 2 BCR BETA-CAROTENE × 2 CU COPPER (II) ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PETN_SPIOL
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–29; UniProt 1–29 Author chain P; PDBConstruct 1–29; UniProt 1–29

Plastocyanin, chloroplastic

OrganismNot specified

UniProt P00289

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 × 17 PDB declaration: 17-meric(17) Consistent with protein copy count Chain Q; UniProt 70–168 Not recorded Cytochrome b6 × 2 (P00165) Cytochrome b6-f complex subunit 4 × 2 (P00166) Cytochrome f × 2 (P16013) Cytochrome b6-f complex iron-sulfur subunit, chloroplastic × 2 (P08980) Cytochrome b6-f complex subunit 6 × 2 (Q9M3L0) Cytochrome b6-f complex subunit 7 × 2 (P80883) Cytochrome b6-f complex subunit 5 × 2 (P69461) Cytochrome b6-f complex subunit 8 × 2 (P61045) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 4 UMQ UNDECYL-MALTOSIDE × 6 PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-BENZOQUINONE × 7 CLA CHLOROPHYLL A × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL × 2 BCR BETA-CAROTENE × 2 CU COPPER (II) ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PLAS_SPIOL
Isoform
PDB entities 9
Chains and sequence ranges Author chain Q; PDBConstruct 1–99; UniProt 70–168

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 9tgg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9tgg
Deposition date deposition_date2025-12-01
Structure title titleCryo-EM structure of Spinacia oleracea cytochrome b6f complex with bound plastocyanin
Keywords keywords;b6f complex, photosynthesis, membrane protein, electron transport, proton transport, quinone catalysis, plastocyanin, OXIDOREDUCTASE ;; OXIDOREDUCTASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.11
Radius of gyration Rg (electron density) rg_electron44.64
Forward intensity I(0) i0644614000.00
Molecular weight molecular_weight237190.0 kDa
Excluded volume excluded_volume308050 ų
Envelope volume envelope_volume429740 ų
Hydration-shell volume shell_volume79142 ų
Envelope diameter envelope_diameter155.5
Shell Rg shell_rg50.21
Envelope Rg envelope_rg44.58
Shape Rg shape_rg44.62
Total Rg total_rg45.00
Total atoms total_atoms16731
Residues n_residues2001
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 dmax147.2
Rg (real space) rg_real46.01
Rg uncertainty (real space) rg_real_error1.17
I(0) (real space) i0_real6.4460e+08
I(0) uncertainty (real space) i0_real_error1.1730e+07
Rg (reciprocal space) rg_reciprocal46.11
I(0) (reciprocal space) i0_reciprocal644700000.0000
Solution quality estimate total_estimate0.6636
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.3
Skewness Skewness skewness0.240
Kurtosis Kurtosis kurtosis-0.471
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha67930000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.939; Stabil: 1.000; Sysdev: 0.021; Positv: 1.000; Valcen: 0.991; Smooth: 0.750

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (18)

8. Citations (1)

9. Files and Curves (10)