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25 hits found for Bartels

SASDW94 – Horse apoferritin from AF4-SAXS measurements

Ferritin light chain experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Ferritin light chain 24-mer, 480 kDa Equus caballus protein
Buffer: phosphate buffered saline, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Jun 19
AF4-to-SAXS: expanded characterization of nanoparticles and proteins at the P12 BioSAXS beamline. J Synchrotron Radiat (2025)
...Bartels K, Franke D, Soloviov D, Gräwert T, Molodenskiy D, Kolb B, Wilhelmy C, Drexel R, Meier F, Haas H, Langguth P, Graewert MA
RgGuinier 5.4 nm
Dmax 13.3 nm
VolumePorod 632 nm3

SASDWA4 – Yeast alcohol dehydrogenase 1 from AF4-SAXS measurements

Alcohol dehydrogenase 1 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Alcohol dehydrogenase 1 tetramer, 147 kDa Saccharomyces cerevisiae (strain … protein
Buffer: phosphate buffered saline, 1% glycerol, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Apr 13
AF4-to-SAXS: expanded characterization of nanoparticles and proteins at the P12 BioSAXS beamline. J Synchrotron Radiat (2025)
...Bartels K, Franke D, Soloviov D, Gräwert T, Molodenskiy D, Kolb B, Wilhelmy C, Drexel R, Meier F, Haas H, Langguth P, Graewert MA
RgGuinier 3.4 nm
Dmax 9.5 nm
VolumePorod 197 nm3

SASDWB4 – Sweet potato beta-amylase from AF4-SAXS measurement

Beta-amylase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Beta-amylase tetramer, 224 kDa Ipomoea batatas protein
Buffer: phosphate buffered saline, 1% glycerol, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Apr 13
AF4-to-SAXS: expanded characterization of nanoparticles and proteins at the P12 BioSAXS beamline. J Synchrotron Radiat (2025)
...Bartels K, Franke D, Soloviov D, Gräwert T, Molodenskiy D, Kolb B, Wilhelmy C, Drexel R, Meier F, Haas H, Langguth P, Graewert MA
RgGuinier 4.2 nm
Dmax 12.6 nm
VolumePorod 297 nm3

SASDWC4 – 100 nm polystyrene beads from AF4-SAXS measurements

Sigma-Aldrich polystyrene nanospheres with a diameter of 100 nm experimental SAS data
Sigma-Aldrich polystyrene nanospheres with a diameter of 100 nm Kratky plot
Sample: Sigma-Aldrich polystyrene nanospheres with a diameter of 100 nm monomer, 0 kDa synthetic construct
Buffer: water/detergent solution (0.0125 % (v/v) NovaChem), pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Jun 19
AF4-to-SAXS: expanded characterization of nanoparticles and proteins at the P12 BioSAXS beamline. J Synchrotron Radiat (2025)
...Bartels K, Franke D, Soloviov D, Gräwert T, Molodenskiy D, Kolb B, Wilhelmy C, Drexel R, Meier F, Haas H, Langguth P, Graewert MA
RgGuinier 47.7 nm
Dmax 111.0 nm

SASDWD4 – 20 nm polystyrene beads from AF4-SAXS measurements

Thermo Fisher polystyrene nanospheres with a diameter of 20 nm experimental SAS data
Thermo Fisher polystyrene nanospheres with a diameter of 20 nm Kratky plot
Sample: Thermo Fisher polystyrene nanospheres with a diameter of 20 nm monomer, 1 kDa synthetic construct
Buffer: water/detergent solution (0.0125 % (v/v) NovaChem), pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Jun 19
AF4-to-SAXS: expanded characterization of nanoparticles and proteins at the P12 BioSAXS beamline. J Synchrotron Radiat (2025)
...Bartels K, Franke D, Soloviov D, Gräwert T, Molodenskiy D, Kolb B, Wilhelmy C, Drexel R, Meier F, Haas H, Langguth P, Graewert MA
RgGuinier 9.0 nm
Dmax 25.0 nm

SASD2F7 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 1

Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 1 experimental SAS data
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 1 Rg histogram
Sample: Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 1 monomer, 36 kDa Chimera protein
Buffer: 50 mM Na-phosphate, 2 mM TCEP, pH: 6
Experiment: SAXS data collected at SWING, SOLEIL on 2024 Oct 17
Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions? Biophysical Journal (2026)
...Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P
RgGuinier 2.7 nm

SASD2G7 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 2

Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 2 experimental SAS data
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 2 Rg histogram
Sample: Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 2 monomer, 36 kDa Chimera protein
Buffer: 50 mM Na-phosphate, 2 mM TCEP, pH: 6
Experiment: SAXS data collected at SWING, SOLEIL on 2024 Oct 17
Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions? Biophysical Journal (2026)
...Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P
RgGuinier 2.8 nm

SASDSH7 – Cationic liposomes containing DOTMA:DOPE (2:1) with negatively charged messenger RNA (mRNA) (raito 0.65:1)

mRNA -- proprietary sequence(R)-N,N,N-trimethyl-2-3-dioleyloxy-1-propanaminium chloride1,2-dioleoyl-sn-glycero-3-phosphoethanolamine experimental SAS data
OTHER [STATIC IMAGE] model
Sample: mRNA -- proprietary sequence , 400 kDa RNA
(R)-N,N,N-trimethyl-2-3-dioleyloxy-1-propanaminium chloride , 1 kDa lipid
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine , 1 kDa lipid
Buffer: 10 mM HEPES, 5 mM NaCl, 0.1 mM EDTA, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2022 Jun 9
Quantitative size-resolved characterization of mRNA nanoparticles by in-line coupling of asymmetrical-flow field-flow fractionation with small angle X-ray scattering. Sci Rep 13(1):15764 (2023)
...Bartels K, Nawroth T, Klein T, Svergun D, Langguth P, Haas H

SASD2H7 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 3

Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 3 experimental SAS data
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 3 Rg histogram
Sample: Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 3 monomer, 36 kDa Chimera protein
Buffer: 50 mM Na-phosphate, 2 mM TCEP, pH: 6
Experiment: SAXS data collected at SWING, SOLEIL on 2025 Mar 13
Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions? Biophysical Journal (2026)
...Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P
RgGuinier 2.7 nm

SASD2J7 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 4

Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 4 experimental SAS data
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 4 Rg histogram
Sample: Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 4 monomer, 36 kDa Chimera protein
Buffer: 50 mM Na-phosphate, 2 mM TCEP, pH: 6
Experiment: SAXS data collected at SWING, SOLEIL on 2024 Oct 17
Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions? Biophysical Journal (2026)
...Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P
RgGuinier 2.7 nm

SASD2K7 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 5

Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 5 experimental SAS data
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 5 Rg histogram
Sample: Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 5 monomer, 36 kDa Chimera protein
Buffer: 50 mM Na-phosphate, 2 mM TCEP, pH: 6
Experiment: SAXS data collected at SWING, SOLEIL on 2025 May 29
Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions? Biophysical Journal (2026)
...Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P
RgGuinier 2.8 nm

SASD2M7 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 6

Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 6 experimental SAS data
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 6 Rg histogram
Sample: Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 6 monomer, 36 kDa Chimera protein
Buffer: 50 mM Na-phosphate, 2 mM TCEP, pH: 6
Experiment: SAXS data collected at SWING, SOLEIL on 2024 Dec 6
Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions? Biophysical Journal (2026)
...Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P
RgGuinier 2.8 nm

SASD2T7 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 7

Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 7 experimental SAS data
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 7 Rg histogram
Sample: Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 7 monomer, 37 kDa Chimera protein
Buffer: 50 mM Na-phosphate, 2 mM TCEP, pH: 6
Experiment: SAXS data collected at SWING, SOLEIL on 2025 Mar 13
Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions? Biophysical Journal (2026)
...Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P
RgGuinier 2.9 nm

SASD2U7 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 8

Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 8 experimental SAS data
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 8 Rg histogram
Sample: Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 8 monomer, 36 kDa Chimera protein
Buffer: 50 mM Na-phosphate, 2 mM TCEP, pH: 6
Experiment: SAXS data collected at SWING, SOLEIL on 2025 Mar 13
Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions? Biophysical Journal (2026)
...Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P
RgGuinier 2.9 nm

SASD2V7 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 9

Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 9 experimental SAS data
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 9 Rg histogram
Sample: Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 9 monomer, 37 kDa Chimera protein
Buffer: 50 mM Na-phosphate, 2 mM TCEP, pH: 6
Experiment: SAXS data collected at SWING, SOLEIL on 2025 Mar 13
Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions? Biophysical Journal (2026)
...Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P
RgGuinier 2.8 nm

SASD2W7 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 10

Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 10 experimental SAS data
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 10 Rg histogram
Sample: Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 10 monomer, 37 kDa Chimera protein
Buffer: 50 mM Na-phosphate, 2 mM TCEP, pH: 6
Experiment: SAXS data collected at SWING, SOLEIL on 2024 Dec 6
Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions? Biophysical Journal (2026)
...Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P
RgGuinier 3.0 nm

SASD2X7 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 11

Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 11 experimental SAS data
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 11 Rg histogram
Sample: Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 11 monomer, 38 kDa Chimera protein
Buffer: 50 mM Na-phosphate, 2 mM TCEP, pH: 6
Experiment: SAXS data collected at SWING, SOLEIL on 2025 Mar 13
Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions? Biophysical Journal (2026)
...Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P
RgGuinier 3.0 nm

SASD2Y7 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 12

Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 12 experimental SAS data
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 12 Rg histogram
Sample: Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 12 monomer, 38 kDa Chimera protein
Buffer: 50 mM Na-phosphate, 2 mM TCEP, pH: 6
Experiment: SAXS data collected at SWING, SOLEIL on 2024 Oct 17
Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions? Biophysical Journal (2026)
...Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P
RgGuinier 3.0 nm

SASD2Z7 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 13

Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 13 experimental SAS data
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 13 Rg histogram
Sample: Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 13 monomer, 38 kDa Chimera protein
Buffer: 50 mM Na-phosphate, 2 mM TCEP, pH: 6
Experiment: SAXS data collected at SWING, SOLEIL on 2025 May 29
Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions? Biophysical Journal (2026)
...Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P
RgGuinier 2.9 nm

SASD228 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 14

Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 14 experimental SAS data
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 14 Rg histogram
Sample: Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 14 monomer, 38 kDa Chimera protein
Buffer: 50 mM Na-phosphate, 2 mM TCEP, pH: 6
Experiment: SAXS data collected at SWING, SOLEIL on 2024 Sep 21
Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions? Biophysical Journal (2026)
...Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P
RgGuinier 3.0 nm

SASD238 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 15

Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 15 experimental SAS data
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 15 Rg histogram
Sample: Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 15 monomer, 38 kDa Chimera protein
Buffer: 50 mM Na-phosphate, 2 mM TCEP, pH: 6
Experiment: SAXS data collected at SWING, SOLEIL on 2024 Sep 21
Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions? Biophysical Journal (2026)
...Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P
RgGuinier 3.3 nm

SASD248 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 16

Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 16 experimental SAS data
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 16 Rg histogram
Sample: Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 16 monomer, 39 kDa Chimera protein
Buffer: 50 mM Na-phosphate, 2 mM TCEP, pH: 6
Experiment: SAXS data collected at SWING, SOLEIL on 2024 Sep 21
Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions? Biophysical Journal (2026)
...Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P
RgGuinier 3.0 nm

SASD258 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 17

Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 17 experimental SAS data
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 17 Rg histogram
Sample: Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 17 monomer, 38 kDa Chimera protein
Buffer: 50 mM Na-phosphate, 2 mM TCEP, pH: 6
Experiment: SAXS data collected at SWING, SOLEIL on 2024 Sep 21
Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions? Biophysical Journal (2026)
...Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P
RgGuinier 3.2 nm

SASD268 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 18

Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 18 experimental SAS data
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 18 Rg histogram
Sample: Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 18 monomer, 45 kDa Chimera protein
Buffer: 50 mM Na-phosphate, 2 mM TCEP, pH: 6
Experiment: SAXS data collected at SWING, SOLEIL on 2024 Sep 21
Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions? Biophysical Journal (2026)
...Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P
RgGuinier 3.3 nm

SASDRQ8 – Bovine serum albumin monomer separated using asymmetric flow field flow fractionation (AFFFF)

Albumin experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Albumin monomer, 66 kDa Bos taurus protein
Buffer: 10 mM HEPES, 5 mM NaCl, 0.1 mM EDTA, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2022 Jun 8
Quantitative size-resolved characterization of mRNA nanoparticles by in-line coupling of asymmetrical-flow field-flow fractionation with small angle X-ray scattering. Sci Rep 13(1):15764 (2023)
...Bartels K, Nawroth T, Klein T, Svergun D, Langguth P, Haas H
RgGuinier 2.9 nm
Dmax 9.0 nm
VolumePorod 104 nm3