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9kch

Cryo-EM structure of inner membrane TolQRA complex in CYMAL-6-Neopentyl Glycol detergent micelles

Method: ELECTRON MICROSCOPY Dmax: 105.3 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Tol-Pal system protein TolQ

Escherichia coli K-12

UniProt P0ABU9

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count Chain A； UniProt 1–230 Chain B； UniProt 1–230 Chain C； UniProt 1–230 Chain D； UniProt 1–230 Chain E； UniProt 1–230 Not recorded Tol-Pal system protein TolR × 2 （P0ABV6） Tol-Pal system protein TolA × 1 （P19934） ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5；Phosphate-buffered saline (PBS) buffer at pH 7.5 (20 mM PBS pH 7.5, 300 mM NaCl) with 20 mM Imidazole and 0.04 mM CYMAL-6 Neopentyl Glycol detergent cryo-EM vitrification conditions：Cryogen ETHANE Resolution 4.19 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.

Other PDB Difference from Current Entry 9KCH Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8ODT Structure of TolQR complex from E.coli Deposited 2023-03-09 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric
Chain A 2–230（229 aa）
Chain B 2–230（229 aa）
Chain C 2–230（229 aa）
Chain D 2–230（229 aa）
Chain E 2–230（229 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；Blot force 10 Blot time 3 sec Wait time 2 sec
Resolution 4.20 Å
9K49 Cryo-EM structure of inner membrane TolQRA complex in CYMAL-6-Neopentyl Glycol detergent micelles Deposited 2024-10-21 Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 1–230（230 aa）
Chain B 1–230（230 aa）
Chain C 1–230（230 aa）
Chain D 1–230（230 aa）
Chain E 1–230（230 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；Phosphate-buffered saline (PBS) buffer at pH 7.5 (20 mM PBS pH 7.5, 300 mM NaCl) with 20 mM Imidazole and 0.04 mM CYMAL-6 Neopentyl Glycol detergent
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
9KPZ Structure of TolQRA complex at pH 5.4 from E.coli Deposited 2024-11-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 2–230（229 aa）
Chain B 2–230（229 aa）
Chain C 2–230（229 aa）
Chain D 2–230（229 aa）
Chain E 2–230（229 aa）
Not recorded 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 7 ELECTRON MICROSCOPY
cryo-EM buffer pH 5.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.18 Å
9KQ0 Structure of TolQRA complex at pH 8.0 from E.coli Deposited 2024-11-24 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 2–230（229 aa）
Chain B 2–230（229 aa）
Chain C 2–230（229 aa）
Chain D 2–230（229 aa）
Chain E 2–230（229 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
9O40 cryo-EM structure of TolQR conformation1 in SMA nanodiscs Deposited 2025-04-08 Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric
Chain A 1–230（230 aa）
Chain B 1–230（230 aa）
Chain C 1–230（230 aa）
Chain D 1–230（230 aa）
Chain E 1–230（230 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.92 Å
9QUQ cryo-EM structure of TolQR conformation2 in SMA nanodiscs Deposited 2025-04-11 Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 1–230（230 aa）
Chain B 1–230（230 aa）
Chain C 1–230（230 aa）
Chain D 1–230（230 aa）
Chain E 1–230（230 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.28 Å
9QVD cryo-EM structure of TolQRA in nanodiscs Deposited 2025-04-11 Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric
Chain A 1–230（230 aa）
Chain B 1–230（230 aa）
Chain C 1–230（230 aa）
Chain D 1–230（230 aa）
Chain E 1–230（230 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.52 Å

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

View Construct and Data Evidence
UniProt name TOLQ_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–230； UniProt 1–230 Author chain B； PDBConstruct 1–230； UniProt 1–230 Author chain C； PDBConstruct 1–230； UniProt 1–230 Author chain D； PDBConstruct 1–230； UniProt 1–230 Author chain E； PDBConstruct 1–230； UniProt 1–230

Tol-Pal system protein TolR

Escherichia coli K-12

UniProt P0ABV6

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count Chain F； UniProt 1–142 Chain G； UniProt 1–142 Not recorded Tol-Pal system protein TolQ × 5 （P0ABU9） Tol-Pal system protein TolA × 1 （P19934） ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5；Phosphate-buffered saline (PBS) buffer at pH 7.5 (20 mM PBS pH 7.5, 300 mM NaCl) with 20 mM Imidazole and 0.04 mM CYMAL-6 Neopentyl Glycol detergent cryo-EM vitrification conditions：Cryogen ETHANE Resolution 4.19 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.

Other PDB Difference from Current Entry 9KCH Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
5BY4 Structure and function of the Escherichia coli Tol-Pal stator protein TolR Deposited 2015-06-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 36–142（107 aa） Fragment：UNP RESIDUES 36-142
Not recorded NA SODIUM ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M Hepes buffer pH 7.5, 1.0 M sodium phosphate and 0.8 M potassium phosphate
Resolution 1.70 Å R-free 0.215
8ODT Structure of TolQR complex from E.coli Deposited 2023-03-09 Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric
Chain F 1–142（142 aa）
Chain G 1–142（142 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；Blot force 10 Blot time 3 sec Wait time 2 sec
Resolution 4.20 Å
9K49 Cryo-EM structure of inner membrane TolQRA complex in CYMAL-6-Neopentyl Glycol detergent micelles Deposited 2024-10-21 Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain F 1–142（142 aa）
Chain G 1–142（142 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；Phosphate-buffered saline (PBS) buffer at pH 7.5 (20 mM PBS pH 7.5, 300 mM NaCl) with 20 mM Imidazole and 0.04 mM CYMAL-6 Neopentyl Glycol detergent
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
9KPZ Structure of TolQRA complex at pH 5.4 from E.coli Deposited 2024-11-24 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 12 PDB declaration: dodecameric
Chain F 1–142（142 aa）
Chain G 1–142（142 aa）
Not recorded 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 7 ELECTRON MICROSCOPY
cryo-EM buffer pH 5.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.18 Å
9KQ0 Structure of TolQRA complex at pH 8.0 from E.coli Deposited 2024-11-24 Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 12 PDB declaration: dodecameric
Chain F 1–142（142 aa）
Chain G 1–142（142 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
9O40 cryo-EM structure of TolQR conformation1 in SMA nanodiscs Deposited 2025-04-08 Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric
Chain F 1–142（142 aa）
Chain G 1–142（142 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.92 Å
9QUQ cryo-EM structure of TolQR conformation2 in SMA nanodiscs Deposited 2025-04-11 Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain F 1–142（142 aa）
Chain G 1–142（142 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.28 Å
9QVD cryo-EM structure of TolQRA in nanodiscs Deposited 2025-04-11 Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric
Chain F 1–142（142 aa）
Chain G 1–142（142 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.52 Å

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TOLR_ECOLI
Isoform —
PDB entities 2
Chains and sequence ranges Author chain F； PDBConstruct 1–142； UniProt 1–142 Author chain G； PDBConstruct 1–142； UniProt 1–142

Tol-Pal system protein TolA

Escherichia coli K-12

UniProt P19934

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count Chain H； UniProt 1–421 Not recorded Tol-Pal system protein TolQ × 5 （P0ABU9） Tol-Pal system protein TolR × 2 （P0ABV6） ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5；Phosphate-buffered saline (PBS) buffer at pH 7.5 (20 mM PBS pH 7.5, 300 mM NaCl) with 20 mM Imidazole and 0.04 mM CYMAL-6 Neopentyl Glycol detergent cryo-EM vitrification conditions：Cryogen ETHANE Resolution 4.19 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.

Other PDB Difference from Current Entry 9KCH Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1S62 Solution structure of the Escherichia coli TolA C-terminal domain Deposited 2004-01-22 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 325–421（97 aa） Fragment：C-terminal domain (residues 325-421)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；300 K；Ionic strength (raw mmCIF value) 100mN NaCl, 50mM NaPO4；Pressure ambient
NMR measurement conditions pH 6.8；300 K；Ionic strength (raw mmCIF value) 50mN NaCl, 50mM NaPO4；Pressure ambient
NMR measurement conditions pH 6.8；300 K；Ionic strength (raw mmCIF value) 500mN NaCl, 50mM NaPO4；Pressure ambient
NMR sample composition 1.4mM U-15N, 100mN NaCl, 50mM NaPO4, 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5mM U-15N,13C, 50mN NaCl, 50mM NaPO4, Complete protease inhibitor (Boehringer), 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 0.7mM U-15N, 500mN NaCl, 50mM NaPO4, 90% H2O, 10% D2O | 90% H2O/10% D2O
Resolution not provided
1TOL FUSION OF N-TERMINAL DOMAIN OF THE MINOR COAT PROTEIN FROM GENE III IN PHAGE M13, AND C-TERMINAL DOMAIN OF E. COLI PROTEIN-TOLA Deposited 1999-05-17 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 295–421（127 aa） Fragment：N-TERMINAL DOMAIN OF MINOR COAT PROTEIN AND C-TERMINAL DOMAIN OF TOLA
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；PROTEIN AT CONCENTRATION 8-12 MG/ML IN 50 MM HEPES (PH=7.5) WITH ADDITION OF DTT C=2MM, WAS CRYSTALLIZED USING VAPOR DIFFUSION FROM THE SITTING OR HANGING DROP, WITH THE SOLUTION CONTAINING 25% PEG4000, 0.08M TRIS (PH=8.5), AND 0.15 M SODIUM ACETATE AS A PRECIPITANT. BEFORE SETTING THE DROPS, PROTEIN SOLUTION WAS MIXED WITH THE PRECIPITANT IN THE RATIO 1:1. CRYSTALS WERE GROWING BEST AT TEMPERATURE 15 DEGREES CELSIUS.
Resolution 1.85 Å R-free 0.293
3QDP Structural characterization of the interaction of colicin A, colicin N, and TolB with TolAIII translocon Deposited 2011-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 302–421（120 aa） Fragment：TolA domain III, residues 302-421
Non-standard monomer：Yes (specific site not provided by mmCIF) NO3 NITRATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.28；293 K；0.2 M NaNO3, 2.2 M ammonium sulphate, pH 5.28, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.15 Å R-free 0.225
3QDR Structural characterization of the interaction of colicin A, colicin N, and TolB with the TolAIII translocon Deposited 2011-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 302–421（120 aa） Fragment：TolA domain III, residues 302-421
Non-standard monomer：Yes (specific site not provided by mmCIF) TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；0.2 M K2HPO4, 2.2 M ammonium sulphate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.65 Å R-free 0.273
9DDM E. coli TolAQR conformation I Deposited 2024-08-28 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric
Chain F 2–421（420 aa）
Chain G 2–421（420 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.94 Å
9DDN E. coli TolAQR conformation II Deposited 2024-08-28 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric
Chain F 2–421（420 aa）
Chain G 2–421（420 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.18 Å
9K49 Cryo-EM structure of inner membrane TolQRA complex in CYMAL-6-Neopentyl Glycol detergent micelles Deposited 2024-10-21 Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain H 1–421（421 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；Phosphate-buffered saline (PBS) buffer at pH 7.5 (20 mM PBS pH 7.5, 300 mM NaCl) with 20 mM Imidazole and 0.04 mM CYMAL-6 Neopentyl Glycol detergent
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
9KPZ Structure of TolQRA complex at pH 5.4 from E.coli Deposited 2024-11-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 12 PDB declaration: dodecameric
Chain H 2–421（420 aa）
Chain I 2–421（420 aa）
Chain J 2–421（420 aa）
Chain K 2–421（420 aa）
Chain L 2–421（420 aa）
Not recorded 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 7 ELECTRON MICROSCOPY
cryo-EM buffer pH 5.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.18 Å
9KQ0 Structure of TolQRA complex at pH 8.0 from E.coli Deposited 2024-11-24 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 12 PDB declaration: dodecameric
Chain H 2–421（420 aa）
Chain I 2–421（420 aa）
Chain J 2–421（420 aa）
Chain K 2–421（420 aa）
Chain L 2–421（420 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
9QUQ cryo-EM structure of TolQR conformation2 in SMA nanodiscs Deposited 2025-04-11 Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain H 1–421（421 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.28 Å
9QVD cryo-EM structure of TolQRA in nanodiscs Deposited 2025-04-11 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric
Chain H 1–421（421 aa）
Chain I 1–421（421 aa）
Chain J 1–421（421 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.52 Å

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TOLA_ECOLI
Isoform —
PDB entities 3
Chains and sequence ranges Author chain H； PDBConstruct 1–421； UniProt 1–421

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 9kch

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9kch
Deposition date deposition_date2024-11-01
Structure title titleCryo-EM structure of inner membrane TolQRA complex in CYMAL-6-Neopentyl Glycol detergent micelles
Keywords keywords;bacteria, outer membrane, lipid homeostasis, phospholipid, inner membrane protein, protein complex structure, proton motive force, stator motor, PROTON TRANSPORT ;; PROTON TRANSPORT
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier34.82 Å
Radius of gyration Rg (electron density) rg_electron34.20 Å
Forward intensity I(0) i0231072000.00
Molecular weight molecular_weight129250.0 kDa
Excluded volume excluded_volume165030 ų
Envelope volume envelope_volume226510 ų
Hydration-shell volume shell_volume54370 ų
Envelope diameter envelope_diameter111.6 Å
Shell Rg shell_rg41.97 Å
Envelope Rg envelope_rg33.45 Å
Shape Rg shape_rg34.19 Å
Total Rg total_rg34.85 Å
Total atoms total_atoms18473
Residues n_residues1161
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax105.3 Å
Rg (real space) rg_real34.68 Å
Rg uncertainty (real space) rg_real_error0.56 Å
I(0) (real space) i0_real2.3110e+08
I(0) uncertainty (real space) i0_real_error3.4010e+06
Rg (reciprocal space) rg_reciprocal34.77 Å
I(0) (reciprocal space) i0_reciprocal231100000.0000
Solution quality estimate total_estimate0.8771
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.5 Å
Skewness Skewness skewness0.207
Kurtosis Kurtosis kurtosis-0.433
Angular range angular_range— – 0.2250 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36670000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.946; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.575
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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8. Citations (1)

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9. Files and Curves (10)