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152 hits found for Konarev

SASDG52 – 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) vesicles: 30 nm filter extrusion

1,2-dimyristoyl-sn-glycero-3-phosphocholine experimental SAS data
OTHER [STATIC IMAGE] model
Sample: 1,2-dimyristoyl-sn-glycero-3-phosphocholine monomer, 1 kDa
Buffer: water, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 9
Restoring structural parameters of lipid mixtures from small-angle X-ray scattering data Journal of Applied Crystallography 54(1) (2021)
Konarev P, Gruzinov A, Mertens H, Svergun D
Dmax 66.0 nm

SASDG62 – 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) vesicles: 50 nm filter extrusion

1,2-dimyristoyl-sn-glycero-3-phosphocholine experimental SAS data
OTHER [STATIC IMAGE] model
Sample: 1,2-dimyristoyl-sn-glycero-3-phosphocholine monomer, 1 kDa
Buffer: water, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 9
Restoring structural parameters of lipid mixtures from small-angle X-ray scattering data Journal of Applied Crystallography 54(1) (2021)
Konarev P, Gruzinov A, Mertens H, Svergun D
Dmax 81.5 nm

SASDG72 – 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) vesicles: 100 nm filter extrusion

1,2-dimyristoyl-sn-glycero-3-phosphocholine experimental SAS data
OTHER [STATIC IMAGE] model
Sample: 1,2-dimyristoyl-sn-glycero-3-phosphocholine monomer, 1 kDa
Buffer: water, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 9
Restoring structural parameters of lipid mixtures from small-angle X-ray scattering data Journal of Applied Crystallography 54(1) (2021)
Konarev P, Gruzinov A, Mertens H, Svergun D
Dmax 111.0 nm

SASDG82 – 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) vesicles: 200 nm filter extrusion

1,2-dimyristoyl-sn-glycero-3-phosphocholine experimental SAS data
OTHER [STATIC IMAGE] model
Sample: 1,2-dimyristoyl-sn-glycero-3-phosphocholine monomer, 1 kDa
Buffer: water, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 9
Restoring structural parameters of lipid mixtures from small-angle X-ray scattering data Journal of Applied Crystallography 54(1) (2021)
Konarev P, Gruzinov A, Mertens H, Svergun D
Dmax 147.0 nm

SASDG92 – 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) vesicles: 30 nm filter extrusion

1,2-dipalmitoyl-sn-glycero-3-phosphocholine experimental SAS data
OTHER [STATIC IMAGE] model
Sample: 1,2-dipalmitoyl-sn-glycero-3-phosphocholine monomer, 1 kDa
Buffer: water, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 9
Restoring structural parameters of lipid mixtures from small-angle X-ray scattering data Journal of Applied Crystallography 54(1) (2021)
Konarev P, Gruzinov A, Mertens H, Svergun D
Dmax 66.0 nm

SASDGA2 – 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) vesicles: 50 nm filter extrusion

1,2-dipalmitoyl-sn-glycero-3-phosphocholine experimental SAS data
OTHER [STATIC IMAGE] model
Sample: 1,2-dipalmitoyl-sn-glycero-3-phosphocholine monomer, 1 kDa
Buffer: water, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 9
Restoring structural parameters of lipid mixtures from small-angle X-ray scattering data Journal of Applied Crystallography 54(1) (2021)
Konarev P, Gruzinov A, Mertens H, Svergun D
Dmax 105.0 nm

SASDGB2 – 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) vesicles: 100 nm filter extrusion

1,2-dipalmitoyl-sn-glycero-3-phosphocholine experimental SAS data
OTHER [STATIC IMAGE] model
Sample: 1,2-dipalmitoyl-sn-glycero-3-phosphocholine monomer, 1 kDa
Buffer: water, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 9
Restoring structural parameters of lipid mixtures from small-angle X-ray scattering data Journal of Applied Crystallography 54(1) (2021)
Konarev P, Gruzinov A, Mertens H, Svergun D
Dmax 112.0 nm

SASDGC2 – 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) vesicles: 200 nm filter extrusion

1,2-dipalmitoyl-sn-glycero-3-phosphocholine experimental SAS data
OTHER [STATIC IMAGE] model
Sample: 1,2-dipalmitoyl-sn-glycero-3-phosphocholine monomer, 1 kDa
Buffer: water, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 9
Restoring structural parameters of lipid mixtures from small-angle X-ray scattering data Journal of Applied Crystallography 54(1) (2021)
Konarev P, Gruzinov A, Mertens H, Svergun D
Dmax 180.0 nm

SASDMR2 – HPMA-Based Nanoparticles with Cholesterol (1.4%)

N-(2-hydroxypropyl)- 31 methacrylamide (HPMA) copolymers with cholesterol 1.4% experimental SAS data
DAMFILT model
Sample: N-(2-hydroxypropyl)- 31 methacrylamide (HPMA) copolymers with cholesterol 1.4% 0, 16272 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Mar 27
Macromolecular HPMA-based nanoparticles with cholesterol for solid-tumor targeting: detailed study of the inner structure of a highly efficient drug delivery system. Biomacromolecules 13(8):2594-604 (2012)
...Konarev PV, Dyakonova M, Papadakis C, Zhigunov A, Plestil J, Stepanek P, Etrych T, Ulbrich K, Svergun DI
RgGuinier 6.2 nm
Dmax 22.0 nm

SASDMS2 – HPMA-Based Nanoparticles with Cholesterol (2.7%)

N-(2-hydroxypropyl)- 31 methacrylamide (HPMA) copolymers with Cholesterol (2.7%) experimental SAS data
DAMFILT model
Sample: N-(2-hydroxypropyl)- 31 methacrylamide (HPMA) copolymers with Cholesterol (2.7%) 0, 16740 kDa
Buffer: phosphate buffer saline (PBS) (pH 7.2), pH: 7.2
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Mar 27
Macromolecular HPMA-based nanoparticles with cholesterol for solid-tumor targeting: detailed study of the inner structure of a highly efficient drug delivery system. Biomacromolecules 13(8):2594-604 (2012)
...Konarev PV, Dyakonova M, Papadakis C, Zhigunov A, Plestil J, Stepanek P, Etrych T, Ulbrich K, Svergun DI
RgGuinier 5.2 nm
Dmax 28.1 nm

SASDMT2 – HPMA-Based Nanoparticles with Cholesterol (3.0%)

N-(2-hydroxypropyl)- 31 methacrylamide (HPMA) copolymers with Cholesterol (3.0%) experimental SAS data
DAMFILT model
Sample: N-(2-hydroxypropyl)- 31 methacrylamide (HPMA) copolymers with Cholesterol (3.0%) 0, 29520 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Mar 27
Macromolecular HPMA-based nanoparticles with cholesterol for solid-tumor targeting: detailed study of the inner structure of a highly efficient drug delivery system. Biomacromolecules 13(8):2594-604 (2012)
...Konarev PV, Dyakonova M, Papadakis C, Zhigunov A, Plestil J, Stepanek P, Etrych T, Ulbrich K, Svergun DI
RgGuinier 9.4 nm
Dmax 43.2 nm

SASDMU2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) without Dox experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) without Dox monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19
Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
...Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 6.1 nm
Dmax 20.5 nm

SASDMV2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) with Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) with Dox (10%) experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) with Dox (10%) monomer, 220 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19
Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
...Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 7.5 nm
Dmax 25.5 nm

SASDMW2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) without Dox experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) without Dox monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19
Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
...Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 6.4 nm
Dmax 22.5 nm

SASDMX2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) with Dox (10%)

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) with Dox (10%) experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) with Dox (10%) monomer, 225 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19
Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
...Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 10.0 nm
Dmax 21.9 nm

SASDBY2 – Inorganic pyrophosphatase (PPase) from E. coli

Inorganic pyrophosphatase (PPase) from E. coli experimental SAS data
DAMMIN model
Sample: Inorganic pyrophosphatase (PPase) from E. coli hexamer, 117 kDa Escherichia coli protein
Buffer: 50 mM Tris 10 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 30
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
...Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 3.0 nm
Dmax 9.0 nm
VolumePorod 166 nm3

SASDMY2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) without Dox experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) without Dox monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19
Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
...Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 6.5 nm
Dmax 22.9 nm

SASDBZ2 – Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli

Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli experimental SAS data
DAMMIN model
Sample: Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli decamer, 381 kDa Escherichia coli protein
Buffer: 50 mM Tris 10 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 30
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
...Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 4.4 nm
Dmax 12.7 nm
VolumePorod 484 nm3

SASDMZ2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) with Dox (10%)

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) with Dox (10%) experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) with Dox (10%) monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19
Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
...Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 6.9 nm
Dmax 23.8 nm

SASDB23 – 5-keto-4-deoxyuronate isomerase (KduI) from E. coli

5-keto-4-deoxyuronate isomerase (KduI) from E. coli experimental SAS data
NONE model
Sample: 5-keto-4-deoxyuronate isomerase (KduI) from E. coli None, Escherichia coli protein
Buffer: 50 mM Tris 10 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 20
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
...Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 4.5 nm

SASDM23 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) without Dox experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) without Dox monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 16
Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
...Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 5.9 nm
Dmax 19.7 nm

SASDB33 – Glutamate decarboxylase alpha (GadA) from E. coli

Glutamate decarboxylase alpha (GadA) from E. coli experimental SAS data
SASREF MX model
Sample: Glutamate decarboxylase alpha (GadA) from E. coli monomer, 53 kDa Escherichia coli protein
Buffer: 50 mM Tris 10 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 20
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
...Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 4.8 nm
VolumePorod 410 nm3

SASDM33 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) with Dox (10%)

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) with Dox (10%) experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) with Dox (10%) monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19
Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
...Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 5.5 nm
Dmax 18.3 nm

SASDN33 – Ternary Human Pex5p(C-terminal)-Pex14p(N)-PTS1 Complex (1:1:1 stoichiometry)

Peroxisomal targeting signal 1 receptor (C -terminal)Peroxisomal membrane protein PEX14 (N-terminal)PTS1-BP experimental SAS data
DAMMIN model
Sample: Peroxisomal targeting signal 1 receptor (C -terminal) monomer, 48 kDa Homo sapiens protein
Peroxisomal membrane protein PEX14 (N-terminal) monomer, 7 kDa Homo sapiens protein
PTS1-BP monomer, 14 kDa Homo sapiens protein
Buffer: 50 mM HEPES-KOH (pH 7.5), 100mM KCl, and 20mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Oct 3
Solution structure of human Pex5.Pex14.PTS1 protein complexes obtained by small angle X-ray scattering. J Biol Chem 284(37):25334-42 (2009)
...Konarev PV, Neufeld C, Wilmanns M, Svergun DI
RgGuinier 2.9 nm
Dmax 9.0 nm
VolumePorod 110 nm3

SASDN43 – Full-length Human Pex5p protein

Peroxisomal targeting signal 1 receptor experimental SAS data
DAMMIN model
Sample: Peroxisomal targeting signal 1 receptor monomer, 71 kDa Homo sapiens protein
Buffer: 50 mM HEPES-KOH (pH 7.5), 100mM KCl, and 20mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Feb 24
Solution structure of human Pex5.Pex14.PTS1 protein complexes obtained by small angle X-ray scattering. J Biol Chem 284(37):25334-42 (2009)
...Konarev PV, Neufeld C, Wilmanns M, Svergun DI
RgGuinier 5.0 nm
Dmax 20.0 nm
VolumePorod 181 nm3

SASDN53 – Ternary Human Pex5p(full-length)-Pex14p(N)-PTS1 Protein Complex (1:7:1 stoichiometry)

Peroxisomal targeting signal 1 receptorPeroxisomal membrane protein PEX14PTS1-BP experimental SAS data
SASREF model
Sample: Peroxisomal targeting signal 1 receptor monomer, 71 kDa Homo sapiens protein
Peroxisomal membrane protein PEX14 monomer, 7 kDa Homo sapiens protein
PTS1-BP monomer, 13 kDa Homo sapiens protein
Buffer: 50 mM HEPES-KOH (pH 7.5), 100mM KCl, and 20mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Mar 18
Solution structure of human Pex5.Pex14.PTS1 protein complexes obtained by small angle X-ray scattering. J Biol Chem 284(37):25334-42 (2009)
...Konarev PV, Neufeld C, Wilmanns M, Svergun DI
RgGuinier 6.0 nm
Dmax 20.0 nm
VolumePorod 267 nm3

SASDM73 – Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 0%)

Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 0%) experimental SAS data
DAMMIN model
Sample: Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 0%) heptamer, 2 kDa
Buffer: water-ethanol solution (water fraction 0%), pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Nov 24
Rigidity, conformation, and solvation of native and oxidized tannin macromolecules in water-ethanol solution. J Chem Phys 130(24):245103 (2009)
...Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 1.0 nm
Dmax 3.5 nm

SASDM83 – Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 60%)

Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 60%) experimental SAS data
DAMMIN model
Sample: Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 60%) heptamer, 2 kDa
Buffer: water-ethanol solution (water fraction 60%), pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Nov 24
Rigidity, conformation, and solvation of native and oxidized tannin macromolecules in water-ethanol solution. J Chem Phys 130(24):245103 (2009)
...Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 1.0 nm
Dmax 3.2 nm

SASDM93 – Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 100%)

Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 100%) experimental SAS data
DAMMIN model
Sample: Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 100%) heptamer, 2 kDa
Buffer: water-ethanol solution (water fraction 100%), pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Nov 24
Rigidity, conformation, and solvation of native and oxidized tannin macromolecules in water-ethanol solution. J Chem Phys 130(24):245103 (2009)
...Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 1.0 nm
Dmax 3.1 nm

SASDN93 – Dystrophiamyotonica kinase (DMPK)

Myotonin-protein kinase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Myotonin-protein kinase monomer, 92 kDa Homo sapiens protein
Buffer: 50 mM TrisHCl 50mM NaCl, 2.5 mM-mercaptoethanol, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Mar 18
Molecular insights into the self‐assembly mechanism of dystrophia myotonica kinase The FASEB Journal 20(8):1142-1151 (2006)
...Konarev P, Marino M, Mayans O
RgGuinier 3.9 nm
Dmax 13.0 nm
VolumePorod 173 nm3

SASDMA3 – Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 100%)

Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 100%) experimental SAS data
DAMMIN model
Sample: Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 100%) heptamer, 2 kDa
Buffer: water-ethanol solution (water fraction 100%), pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Oct 12
Rigidity, conformation, and solvation of native and oxidized tannin macromolecules in water-ethanol solution. J Chem Phys 130(24):245103 (2009)
...Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 1.0 nm
Dmax 3.3 nm

SASDMB3 – Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 80%)

Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 80%) experimental SAS data
DAMMIN model
Sample: Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 80%) heptamer, 2 kDa
Buffer: water-ethanol solution (water fraction 80%), pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Nov 24
Rigidity, conformation, and solvation of native and oxidized tannin macromolecules in water-ethanol solution. J Chem Phys 130(24):245103 (2009)
...Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 0.9 nm
Dmax 3.3 nm

SASDMC3 – Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 0%)

Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 0%) experimental SAS data
DAMMIN model
Sample: Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 0%) heptamer, 2 kDa
Buffer: water-ethanol solution (water fraction 0%), pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Nov 24
Rigidity, conformation, and solvation of native and oxidized tannin macromolecules in water-ethanol solution. J Chem Phys 130(24):245103 (2009)
...Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 1.3 nm
Dmax 4.5 nm

SASDMD3 – Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 20%)

Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 20%) experimental SAS data
DAMMIN model
Sample: Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 20%) heptamer, 2 kDa
Buffer: water-ethanol solution (water fraction 20%), pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Nov 24
Rigidity, conformation, and solvation of native and oxidized tannin macromolecules in water-ethanol solution. J Chem Phys 130(24):245103 (2009)
...Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 1.1 nm
Dmax 3.5 nm

SASDME3 – Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 60%)

Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 60%) experimental SAS data
DAMMIN model
Sample: Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 60%) heptamer, 2 kDa
Buffer: water-ethanol solution (water fraction 60%), pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Nov 24
Rigidity, conformation, and solvation of native and oxidized tannin macromolecules in water-ethanol solution. J Chem Phys 130(24):245103 (2009)
...Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 1.0 nm
Dmax 2.9 nm

SASDMF3 – Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 80%)

Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 80%) experimental SAS data
DAMMIN model
Sample: Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 80%) heptamer, 2 kDa
Buffer: water-ethanol solution (water fraction 80%), pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Oct 12
Rigidity, conformation, and solvation of native and oxidized tannin macromolecules in water-ethanol solution. J Chem Phys 130(24):245103 (2009)
...Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 1.2 nm
Dmax 3.6 nm

SASDAS3 – Fila16-17

immunoglobulin- like filamin two-domain fragment 16-17 experimental SAS data
GASBOR model
Sample: immunoglobulin- like filamin two-domain fragment 16-17 monomer, 19 kDa Escherichia coli protein
Buffer: 100 mM NaCl 10 mM dithiothreitol 20 mM Tris, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Jun 18
Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin. J Biol Chem 284(37):25450-8 (2009)
...Konarev PV, Svergun DI, Iivanainen T, Heikkinen SM, Permi P, Koskela H, Kilpeläinen I, Ylänne J
RgGuinier 1.9 nm
Dmax 6.0 nm
VolumePorod 33 nm3

SASDAT3 – Fila18-19

immunoglobulin- like filamin two-domain fragment 18-19 experimental SAS data
GASBOR model
Sample: immunoglobulin- like filamin two-domain fragment 18-19 monomer, 20 kDa Escherichia coli protein
Buffer: 100 mM NaCl 10 mM dithiothreitol 20 mM Tris, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Jun 18
Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin. J Biol Chem 284(37):25450-8 (2009)
...Konarev PV, Svergun DI, Iivanainen T, Heikkinen SM, Permi P, Koskela H, Kilpeläinen I, Ylänne J
RgGuinier 2.1 nm
Dmax 6.5 nm
VolumePorod 34 nm3

SASDAU3 – Fila22-23

immunoglobulin- like filamin two-domain fragment 22-23 experimental SAS data
GASBOR model
Sample: immunoglobulin- like filamin two-domain fragment 22-23 monomer, 19 kDa Escherichia coli protein
Buffer: 100 mM NaCl 10 mM dithiothreitol 20 mM Tris, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Jun 18
Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin. J Biol Chem 284(37):25450-8 (2009)
...Konarev PV, Svergun DI, Iivanainen T, Heikkinen SM, Permi P, Koskela H, Kilpeläinen I, Ylänne J
RgGuinier 2.8 nm
Dmax 9.0 nm
VolumePorod 32 nm3

SASDA54 – RNA Aptamer

SRB2m experimental SAS data
DAMMIN model
Sample: SRB2m dimer, 33 kDa RNA
Buffer: Hepes, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Oct 24
Characterization of a fluorophore binding RNA aptamer by fluorescence correlation spectroscopy and small angle X-ray scattering. Anal Biochem 389(1):52-62 (2009)
...Konarev PV, Svergun DI, Hahn U
RgGuinier 2.8 nm
Dmax 10.0 nm
VolumePorod 38 nm3

SASDA74 – RNA Aptamer

SRB2m experimental SAS data
DAMMIN model
Sample: SRB2m dimer, 33 kDa RNA
Buffer: Hepes, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Oct 24
Characterization of a fluorophore binding RNA aptamer by fluorescence correlation spectroscopy and small angle X-ray scattering. Anal Biochem 389(1):52-62 (2009)
...Konarev PV, Svergun DI, Hahn U
RgGuinier 2.4 nm
Dmax 8.5 nm
VolumePorod 31 nm3

SASDA84 – RNA Aptamer

SRB2m experimental SAS data
DAMMIN model
Sample: SRB2m dimer, 33 kDa RNA
Buffer: Hepes, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Oct 24
Characterization of a fluorophore binding RNA aptamer by fluorescence correlation spectroscopy and small angle X-ray scattering. Anal Biochem 389(1):52-62 (2009)
...Konarev PV, Svergun DI, Hahn U
RgGuinier 2.3 nm
Dmax 8.0 nm
VolumePorod 24 nm3

SASDA94 – Der p21

Der p21, allegren experimental SAS data
DAMMIN model
Sample: Der p21, allegren dimer, 26 kDa Escherichia coli protein
Buffer: 10 mM Hepes , pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Jul 24
Characterization of Der p 21, a new important allergen derived from the gut of house dust mites. Allergy 63(6):758-67 (2008)
...Konarev PV, Valent P, Thalhamer J, Keller W, Valenta R, Vrtala S
RgGuinier 2.7 nm
Dmax 8.5 nm
VolumePorod 50 nm3

SASDAA4 – Full length GbpA

Full length GbpA experimental SAS data
GASBOR model
Sample: Full length GbpA monomer, 54 kDa Vibrio cholerae protein
Buffer: 25 mM Tris/HCl 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Oct 16
The Vibrio cholerae colonization factor GbpA possesses a modular structure that governs binding to different host surfaces. PLoS Pathog 8(1):e1002373 (2012)
...Konarev PV, Ibrahim AF, Svergun DI, Eijsink VG, Chatterjee NS, van Aalten DM
RgGuinier 3.9 nm
Dmax 14.5 nm
VolumePorod 100 nm3

SASDAB4 – Truncated GbpA

Truncated GbpA experimental SAS data
GASBOR model
Sample: Truncated GbpA monomer, 44 kDa Vibrio cholerae protein
Buffer: 25 mM Tris/HCl 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Oct 16
The Vibrio cholerae colonization factor GbpA possesses a modular structure that governs binding to different host surfaces. PLoS Pathog 8(1):e1002373 (2012)
...Konarev PV, Ibrahim AF, Svergun DI, Eijsink VG, Chatterjee NS, van Aalten DM
RgGuinier 3.6 nm
Dmax 12.5 nm
VolumePorod 80 nm3

SASDAC4 – FilaminC 23-24

Filamin C 23-24 experimental SAS data
DAMMIN model
Sample: Filamin C 23-24 dimer, 40 kDa Escherichia coli protein
Buffer: 20 mM Tris-HCl 50 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Jun 17
Crystal structure of human filamin C domain 23 and small angle scattering model for filamin C 23-24 dimer. J Mol Biol 368(4):1011-23 (2007)
...Konarev P, Carugo O, Rybin V, Kiema TR, Svergun D, Ylänne J, Djinović Carugo K
RgGuinier 3.5 nm
Dmax 13.0 nm
VolumePorod 75 nm3

SASDAD4 – Full length GtBP3

full length CtBP3 experimental SAS data
DAMMIN model
Sample: full length CtBP3 tetramer, 170 kDa protein
Buffer: 25 mM Tris/HCl 250 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2004 Nov 18
The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured. Protein Sci 15(5):1042-50 (2006)
...Konarev PV, Spanò S, Fasano M, Bracco C, Pesce A, Donadini A, Cericola C, Secundo F, Luini A, Corda D, Bolognesi M
RgGuinier 5.1 nm
Dmax 19.0 nm
VolumePorod 330 nm3

SASDAE4 – C-terminal CtBP3

C-term part CtBP3 experimental SAS data
DAMMIN model
Sample: C-term part CtBP3 dimer, 52 kDa protein
Buffer: 25 mM Tris/HCl 250 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2004 Nov 18
The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured. Protein Sci 15(5):1042-50 (2006)
...Konarev PV, Spanò S, Fasano M, Bracco C, Pesce A, Donadini A, Cericola C, Secundo F, Luini A, Corda D, Bolognesi M
RgGuinier 5.5 nm
Dmax 20.0 nm
VolumePorod 126 nm3

SASDBS4 – Glutamate decarboxylase alpha (GadA) from E. coli, low salt

Glutamate decarboxylase alpha (GadA) from E. coli experimental SAS data
SASREF MX model
Sample: Glutamate decarboxylase alpha (GadA) from E. coli monomer, 53 kDa Escherichia coli protein
Buffer: 50 mM Tris, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jul 29
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
...Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 4.4 nm
VolumePorod 450 nm3

SASDA55 – Nucleoplasmin

Nucleoplasmin experimental SAS data
BUNCH model
Sample: Nucleoplasmin pentamer, 110 kDa Escherichia coli protein
Buffer: 20 mM Pipes buffer 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Dec 3
A mechanism for histone chaperoning activity of nucleoplasmin: thermodynamic and structural models. J Mol Biol 393(2):448-63 (2009)
...Konarev PV, Svergun DI, Velázquez-Campoy A, Urbaneja MA
RgGuinier 4.0 nm
Dmax 12.6 nm
VolumePorod 210 nm3

SASDA65 – Nucleoplasmin-H5 complex

NP-H5 experimental SAS data
MONSA model
Sample: NP-H5 pentamer, 200 kDa Escherichia coli protein
Buffer: 20 mM Pipes buffer 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Dec 3
A mechanism for histone chaperoning activity of nucleoplasmin: thermodynamic and structural models. J Mol Biol 393(2):448-63 (2009)
...Konarev PV, Svergun DI, Velázquez-Campoy A, Urbaneja MA
RgGuinier 5.2 nm
Dmax 16.7 nm
VolumePorod 410 nm3

SASDA75 – Nucleoplasmin-H2AH2B complex

NP-H2AH2B experimental SAS data
MONSA model
Sample: NP-H2AH2B pentamer, 250 kDa Escherichia coli protein
Buffer: 20 mM Pipes buffer 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2014 Dec 3
A mechanism for histone chaperoning activity of nucleoplasmin: thermodynamic and structural models. J Mol Biol 393(2):448-63 (2009)
...Konarev PV, Svergun DI, Velázquez-Campoy A, Urbaneja MA
RgGuinier 4.7 nm
Dmax 14.5 nm
VolumePorod 470 nm3

SASDC95 – Light encoded DNA biosensor: e14A DNA

e14A experimental SAS data
DAMMIF model
Sample: e14A monomer, 21 kDa DNA
Buffer: 154 mM NaCl, pH: 8.3
Experiment: SAXS data collected at BM29, ESRF on 2016 Jun 16
Optical and Structural Characterization of a Chronic Myeloid Leukemia DNA Biosensor. ACS Chem Biol 13(5):1235-1242 (2018)
...Konarev PV, Lima JC, Santos-Silva T, Baptista PV
RgGuinier 2.8 nm
Dmax 12.5 nm

SASDCA5 – Light encoded DNA biosensor: e14B DNA

e14B experimental SAS data
DAMMIF model
Sample: e14B monomer, 13 kDa DNA
Buffer: 154 mM NaCl, pH: 8.3
Experiment: SAXS data collected at BM29, ESRF on 2016 Jun 16
Optical and Structural Characterization of a Chronic Myeloid Leukemia DNA Biosensor. ACS Chem Biol 13(5):1235-1242 (2018)
...Konarev PV, Lima JC, Santos-Silva T, Baptista PV
RgGuinier 1.9 nm
Dmax 9.0 nm

SASDCB5 – Light encoded DNA biosensor: e14C DNA

e14C experimental SAS data
DAMFILT model
Sample: e14C monomer, 5 kDa DNA
Buffer: 154 mM NaCl, pH: 8.3
Experiment: SAXS data collected at BM29, ESRF on 2016 Jun 16
Optical and Structural Characterization of a Chronic Myeloid Leukemia DNA Biosensor. ACS Chem Biol 13(5):1235-1242 (2018)
...Konarev PV, Lima JC, Santos-Silva T, Baptista PV
RgGuinier 1.3 nm
Dmax 5.0 nm

SASDAC5 – ImportinA_ImportinB

ImportinA_ImportinB experimental SAS data
DAMMIF model
Sample: ImportinA_ImportinB monomer, 160 kDa Escherichia coli protein
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Oct 29
Recognition of nucleoplasmin by its nuclear transport receptor importin α/β: insights into a complete import complex. Biochemistry 49(45):9756-69 (2010)
...Konarev PV, Urbaneja MA, Svergun DI, Taneva SG, Bañuelos S
RgGuinier 5.7 nm
Dmax 19.0 nm
VolumePorod 390 nm3

SASDCC5 – Light encoded DNA biosensor: e14AB DNA

e14AB experimental SAS data
DAMFILT model
Sample: e14AB monomer, 93 kDa DNA
Buffer: 154 mM NaCl, pH: 8.3
Experiment: SAXS data collected at BM29, ESRF on 2016 Jun 16
Optical and Structural Characterization of a Chronic Myeloid Leukemia DNA Biosensor. ACS Chem Biol 13(5):1235-1242 (2018)
...Konarev PV, Lima JC, Santos-Silva T, Baptista PV
RgGuinier 5.4 nm
Dmax 24.7 nm

SASDAD5 – Nucleoplasmin_ImpA_ImpB

Nucleoplasmin_importinA_importinB experimental SAS data
DAMMIF model
Sample: Nucleoplasmin_importinA_importinB , 900 kDa Escherichia coli protein
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 May 23
Recognition of nucleoplasmin by its nuclear transport receptor importin α/β: insights into a complete import complex. Biochemistry 49(45):9756-69 (2010)
...Konarev PV, Urbaneja MA, Svergun DI, Taneva SG, Bañuelos S
RgGuinier 8.6 nm
Dmax 28.0 nm
VolumePorod 1800 nm3

SASDCD5 – Light encoded DNA biosensor: e14ABC DNA

e14ABC experimental SAS data
DAMFILT model
Sample: e14ABC monomer, 106 kDa DNA
Buffer: 154 mM NaCl, pH: 8.3
Experiment: SAXS data collected at BM29, ESRF on 2016 Jun 16
Optical and Structural Characterization of a Chronic Myeloid Leukemia DNA Biosensor. ACS Chem Biol 13(5):1235-1242 (2018)
...Konarev PV, Lima JC, Santos-Silva T, Baptista PV
RgGuinier 4.7 nm
Dmax 25.0 nm
VolumePorod 152 nm3

SASDCE5 – Light encoded DNA biosensor: e13A DNA

e13A experimental SAS data
DAMFILT model
Sample: e13A monomer, 17 kDa DNA
Buffer: 154 mM NaCl, pH: 8.3
Experiment: SAXS data collected at BM29, ESRF on 2013 Nov 22
Optical and Structural Characterization of a Chronic Myeloid Leukemia DNA Biosensor. ACS Chem Biol 13(5):1235-1242 (2018)
...Konarev PV, Lima JC, Santos-Silva T, Baptista PV
RgGuinier 2.3 nm
Dmax 8.0 nm
VolumePorod 24 nm3

SASDCF5 – Light encoded DNA biosensor: e13B DNA

e13B experimental SAS data
DAMFILT model
Sample: e13B monomer, 10 kDa DNA
Buffer: 154 mM NaCl, pH: 8.3
Experiment: SAXS data collected at BM29, ESRF on 2013 Nov 22
Optical and Structural Characterization of a Chronic Myeloid Leukemia DNA Biosensor. ACS Chem Biol 13(5):1235-1242 (2018)
...Konarev PV, Lima JC, Santos-Silva T, Baptista PV
RgGuinier 1.8 nm
Dmax 7.0 nm
VolumePorod 13 nm3

SASDMF5 – Two-component synthetic liposomes composed of 10% DOPS + 90% DOPC lipid mixtures loaded with M1 protein

Two-component synthetic liposomes composed of 10% DOPS + 90% DOPC lipid mixtures loaded with M1 protein ((lipid:M1 molar ratio 20:1) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Two-component synthetic liposomes composed of 10% DOPS + 90% DOPC lipid mixtures loaded with M1 protein ((lipid:M1 molar ratio 20:1) monomer, 2000 kDa
Buffer: 100 mM NaCl, 50 mM MES buffer, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Oct 30
The Cytoplasmic Tail of Influenza A Virus Hemagglutinin and Membrane Lipid Composition Change the Mode of M1 Protein Association with the Lipid Bilayer Membranes 11(10):772 (2021)
...Konarev P, Fedorova N, Shtykova E, Ksenofontov A, Loshkarev N, Dadinova L, Timofeeva T, Abramchuk S, Moiseenko A, Baratova L, Svergun D, Batishchev O

SASDAG5 – RNA shaperone Hfq

RNA chaperone Hfq experimental SAS data
DAMMIN model
Sample: RNA chaperone Hfq hexamer, 67 kDa Escherichia coli protein
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 May 2
Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq. Nucleic Acids Res 39(11):4900-15 (2011)
...Konarev PV, Sjöblom B, Kloiber K, Hämmerle H, Rajkowitsch L, Miles AJ, Kontaxis G, Wallace BA, Svergun DI, Konrat R, Bläsi U, Djinovic-Carugo K
RgGuinier 3.2 nm
Dmax 11.2 nm
VolumePorod 110 nm3

SASDCG5 – Light encoded DNA biosensor: e13C DNA

e13C experimental SAS data
DAMFILT model
Sample: e13C monomer, 6 kDa DNA
Buffer: 154 mM NaCl, pH: 8.3
Experiment: SAXS data collected at BM29, ESRF on 2013 Nov 22
Optical and Structural Characterization of a Chronic Myeloid Leukemia DNA Biosensor. ACS Chem Biol 13(5):1235-1242 (2018)
...Konarev PV, Lima JC, Santos-Silva T, Baptista PV
RgGuinier 1.3 nm
Dmax 5.0 nm
VolumePorod 8 nm3

SASDDG5 – Mammalian prion protein mRNA (PrP mRNA wild type)

octo-repeat PrP mRNA experimental SAS data
DAMFILT model
Sample: octo-repeat PrP mRNA dimer, 144 kDa human PrP ORF RNA
Buffer: 10 mM Tris buffer, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Nov 4
Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes. Sci Rep 9(1):2465 (2019)
...Konarev PV, Goebel I, Svergun DI, Wills PR, Ignatova Z
RgGuinier 7.4 nm
Dmax 25.0 nm
VolumePorod 165 nm3

SASDLG5 – Human nerve growth factor

Beta-nerve growth factor experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Beta-nerve growth factor dimer, 24 kDa Homo sapiens protein
Buffer: 50 mM Na-phosphate, 1 mM EDTA, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Jul 2
The conundrum of the high-affinity NGF binding site formation unveiled? Biophys J 108(3):687-97 (2015)
...Konarev PV, Cassetta A, Paoletti F, Svergun DI, Lamba D, Cattaneo A
RgGuinier 2.5 nm

SASDMG5 – Two-component synthetic liposomes composed of 30% DOPS + 70% DOPC lipid mixtures loaded with M1 protein

Two-component synthetic liposomes composed of 30% DOPS + 70% DOPC lipid mixtures loaded with M1 protein (lipid:M1 molar ration 20:1) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Two-component synthetic liposomes composed of 30% DOPS + 70% DOPC lipid mixtures loaded with M1 protein (lipid:M1 molar ration 20:1) monomer, 2000 kDa
Buffer: 100 mM NaCl, 50 mM MES buffer, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Oct 31
The Cytoplasmic Tail of Influenza A Virus Hemagglutinin and Membrane Lipid Composition Change the Mode of M1 Protein Association with the Lipid Bilayer Membranes 11(10):772 (2021)
...Konarev P, Fedorova N, Shtykova E, Ksenofontov A, Loshkarev N, Dadinova L, Timofeeva T, Abramchuk S, Moiseenko A, Baratova L, Svergun D, Batishchev O

SASDAH5 – Complex of Hfq with DsrA

RNA chaperone HfqRNA DsrA experimental SAS data
SASREF model
Sample: RNA chaperone Hfq hexamer, 67 kDa Escherichia coli protein
RNA DsrA monomer, 12 kDa RNA
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Nov 16
Structural flexibility of RNA as molecular basis for Hfq chaperone function. Nucleic Acids Res 40(16):8072-84 (2012)
...Konarev PV, Shang W, Vecerek B, Kontaxis G, Hämmerle H, Peterlik H, Svergun DI, Bläsi U, Djinović-Carugo K
RgGuinier 4.3 nm
Dmax 14.5 nm
VolumePorod 210 nm3

SASDCH5 – Light encoded DNA biosensor: e13AB DNA

e13AB experimental SAS data
DAMFILT model
Sample: e13AB monomer, 79 kDa DNA
Buffer: 154 mM NaCl, pH: 8.3
Experiment: SAXS data collected at BM29, ESRF on 2013 Nov 22
Optical and Structural Characterization of a Chronic Myeloid Leukemia DNA Biosensor. ACS Chem Biol 13(5):1235-1242 (2018)
...Konarev PV, Lima JC, Santos-Silva T, Baptista PV
RgGuinier 4.7 nm
Dmax 20.0 nm
VolumePorod 103 nm3

SASDDH5 – Mammalian prion protein mRNA (PrP mRNA wild type) with KCl

octo-repeat PrP mRNA experimental SAS data
DAMFILT model
Sample: octo-repeat PrP mRNA dimer, 144 kDa human PrP ORF RNA
Buffer: 10 mM Tris buffer with 100 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Jun 6
Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes. Sci Rep 9(1):2465 (2019)
...Konarev PV, Goebel I, Svergun DI, Wills PR, Ignatova Z
RgGuinier 8.8 nm
Dmax 31.0 nm
VolumePorod 240 nm3

SASDLH5 – Aggregation state of Ataxin-3 protein

Ataxin-3 experimental SAS data
DAMMIN model
Sample: Ataxin-3 monomer, 41 kDa Homo sapiens protein
Buffer: phosphate buffered saline (PBS), pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Dec 3
Interactions of ataxin-3 with its molecular partners in the protein machinery that sorts protein aggregates to the aggresome. Int J Biochem Cell Biol 51:58-64 (2014)
...Konarev PV, Invernizzi G, Svergun DI, Vanoni M, Regonesi ME, Tortora P
RgGuinier 6.9 nm
Dmax 25.0 nm
VolumePorod 425 nm3

SASDMH5 – Four-component synthetic liposomes composed of 30% bPS + 10% POPC + 40% SM + 20% Chol lipid mixtures loaded with M1 protein

Four-component synthetic liposomes composed of 30% bPS + 10% POPC + 40% SM + 20% Chol lipid mixtures loaded with M1 protein (lipid:M1 molar ration 20:1) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Four-component synthetic liposomes composed of 30% bPS + 10% POPC + 40% SM + 20% Chol lipid mixtures loaded with M1 protein (lipid:M1 molar ration 20:1) monomer, 2000 kDa
Buffer: 100 mM NaCl, 50 mM MES buffer, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Oct 31
The Cytoplasmic Tail of Influenza A Virus Hemagglutinin and Membrane Lipid Composition Change the Mode of M1 Protein Association with the Lipid Bilayer Membranes 11(10):772 (2021)
...Konarev P, Fedorova N, Shtykova E, Ksenofontov A, Loshkarev N, Dadinova L, Timofeeva T, Abramchuk S, Moiseenko A, Baratova L, Svergun D, Batishchev O

SASDCJ5 – Light encoded DNA biosensor: e13ABC DNA

e13ABC experimental SAS data
DAMFILT model
Sample: e13ABC monomer, 42 kDa DNA
Buffer: 154 mM NaCl, pH: 8.3
Experiment: SAXS data collected at BM29, ESRF on 2013 Nov 22
Optical and Structural Characterization of a Chronic Myeloid Leukemia DNA Biosensor. ACS Chem Biol 13(5):1235-1242 (2018)
...Konarev PV, Lima JC, Santos-Silva T, Baptista PV
RgGuinier 3.9 nm
Dmax 18.0 nm
VolumePorod 59 nm3

SASDDJ5 – Mammalian prion protein mRNA (PrP mRNA wild type) with LiCl

octo-repeat PrP mRNA experimental SAS data
DAMFILT model
Sample: octo-repeat PrP mRNA dimer, 144 kDa human PrP ORF RNA
Buffer: 10 mM Tris buffer with 100 mM LiCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Jun 6
Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes. Sci Rep 9(1):2465 (2019)
...Konarev PV, Goebel I, Svergun DI, Wills PR, Ignatova Z
RgGuinier 9.0 nm
Dmax 31.0 nm
VolumePorod 225 nm3

SASDLJ5 – Aggregation state of tubulin protein

Tubulin alpha-1A chain experimental SAS data
DAMMIN model
Sample: Tubulin alpha-1A chain monomer, 50 kDa Homo sapiens protein
Buffer: phosphate buffered saline (PBS), pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Dec 3
Interactions of ataxin-3 with its molecular partners in the protein machinery that sorts protein aggregates to the aggresome. Int J Biochem Cell Biol 51:58-64 (2014)
...Konarev PV, Invernizzi G, Svergun DI, Vanoni M, Regonesi ME, Tortora P
RgGuinier 7.0 nm
Dmax 25.0 nm
VolumePorod 340 nm3

SASDMJ5 – Four-component synthetic liposomes composed of 20% bPS + 13.3% POPC + 33.3% SM + 33.3% Chol lipid mixtures loaded with M1 protein

Four-component synthetic liposomes composed of 20% bPS + 13.3% POPC + 33.3% SM + 33.3% Chol lipid mixtures loaded with M1 protein (lipid:M1 molar ration 20:1) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Four-component synthetic liposomes composed of 20% bPS + 13.3% POPC + 33.3% SM + 33.3% Chol lipid mixtures loaded with M1 protein (lipid:M1 molar ration 20:1) monomer, 2000 kDa
Buffer: 100 mM NaCl, 50 mM MES buffer, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Oct 31
The Cytoplasmic Tail of Influenza A Virus Hemagglutinin and Membrane Lipid Composition Change the Mode of M1 Protein Association with the Lipid Bilayer Membranes 11(10):772 (2021)
...Konarev P, Fedorova N, Shtykova E, Ksenofontov A, Loshkarev N, Dadinova L, Timofeeva T, Abramchuk S, Moiseenko A, Baratova L, Svergun D, Batishchev O

SASDCK5 – Light encoded DNA biosensor: e13Ae14Be13C DNA

e13Ae14Be13C experimental SAS data
DAMFILT model
Sample: e13Ae14Be13C monomer, 40 kDa DNA
Buffer: 154 mM NaCl, pH: 8.3
Experiment: SAXS data collected at BM29, ESRF on 2016 Jun 16
Optical and Structural Characterization of a Chronic Myeloid Leukemia DNA Biosensor. ACS Chem Biol 13(5):1235-1242 (2018)
...Konarev PV, Lima JC, Santos-Silva T, Baptista PV
RgGuinier 3.7 nm
Dmax 18.0 nm
VolumePorod 65 nm3

SASDDK5 – Mammalian prion protein mRNA (PrP mRNA wild type) with KCl and pyridostatin (PDS)

octo-repeat PrP mRNA experimental SAS data
DAMFILT model
Sample: octo-repeat PrP mRNA dimer, 144 kDa human PrP ORF RNA
Buffer: 10 mM Tris buffer with 100 mM KCl and 1 mM PDS, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Jun 6
Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes. Sci Rep 9(1):2465 (2019)
...Konarev PV, Goebel I, Svergun DI, Wills PR, Ignatova Z
RgGuinier 9.1 nm
Dmax 31.0 nm
VolumePorod 220 nm3

SASDLK5 – Aggregation state of ataxin-3-tubulin complex

Ataxin-3Tubulin alpha-1A chain experimental SAS data
DAMMIN model
Sample: Ataxin-3 monomer, 41 kDa Homo sapiens protein
Tubulin alpha-1A chain monomer, 50 kDa Homo sapiens protein
Buffer: phosphate buffered saline (PBS), pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Dec 3
Interactions of ataxin-3 with its molecular partners in the protein machinery that sorts protein aggregates to the aggresome. Int J Biochem Cell Biol 51:58-64 (2014)
...Konarev PV, Invernizzi G, Svergun DI, Vanoni M, Regonesi ME, Tortora P
RgGuinier 8.4 nm
Dmax 30.0 nm
VolumePorod 900 nm3

SASDMK5 – Native liposomes composed of lipids extracted from A/Puerto Rico/8/34 (H1N1) virus envelope loaded with M1 protein.

Native liposomes composed of lipids extracted from A/Puerto Rico/8/34 (H1N1) virus envelope loaded with M1 protein. (lipid:M1 molar ration 4:1) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Native liposomes composed of lipids extracted from A/Puerto Rico/8/34 (H1N1) virus envelope loaded with M1 protein. (lipid:M1 molar ration 4:1) monomer, 2000 kDa
Buffer: 100 mM NaCl, 50 mM MES buffer, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Nov 26
The Cytoplasmic Tail of Influenza A Virus Hemagglutinin and Membrane Lipid Composition Change the Mode of M1 Protein Association with the Lipid Bilayer Membranes 11(10):772 (2021)
...Konarev P, Fedorova N, Shtykova E, Ksenofontov A, Loshkarev N, Dadinova L, Timofeeva T, Abramchuk S, Moiseenko A, Baratova L, Svergun D, Batishchev O

SASDCL5 – Light encoded DNA biosensor: e14Ae13Be14C DNA

e14Ae13Be14C experimental SAS data
DAMFILT model
Sample: e14Ae13Be14C monomer, 31 kDa DNA
Buffer: 154 mM NaCl, pH: 8.3
Experiment: SAXS data collected at BM29, ESRF on 2016 Jun 16
Optical and Structural Characterization of a Chronic Myeloid Leukemia DNA Biosensor. ACS Chem Biol 13(5):1235-1242 (2018)
...Konarev PV, Lima JC, Santos-Silva T, Baptista PV
RgGuinier 3.4 nm
Dmax 14.0 nm
VolumePorod 42 nm3

SASDDL5 – Mutant mammalian prion protein mRNA (octo-repeat PrP mRNA)

octo-repeat PrP mRNA mutant experimental SAS data
DAMFILT model
Sample: octo-repeat PrP mRNA mutant dimer, 144 kDa human PrP ORF RNA
Buffer: 10 mM Tris buffer, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Jun 6
Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes. Sci Rep 9(1):2465 (2019)
...Konarev PV, Goebel I, Svergun DI, Wills PR, Ignatova Z
RgGuinier 7.0 nm
Dmax 24.0 nm
VolumePorod 150 nm3

SASDLL5 – frataxin homolog, Yfh1, at 0 °C

Frataxin homolog, mitochondrial experimental SAS data
frataxin homolog, Yfh1, at 0 °C Rg histogram
Sample: Frataxin homolog, mitochondrial monomer, 14 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 20 mM HEPES, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Nov 28
The role of hydration in protein stability: comparison of the cold and heat unfolded states of Yfh1. J Mol Biol 417(5):413-24 (2012)
...Konarev PV, Svergun DI, Daura X, Temussi P, Pastore A
RgGuinier 2.2 nm

SASDML5 – Proteoliposomes composed of lipids from A/Puerto Rico/8/34 (H1N1) virus envelope together with the HA LI45 peptides loaded with M1 protein

Proteoliposomes composed of lipids from A/Puerto Rico/8/34 (H1N1) virus envelope together with the HA LI45 peptides loaded with M1 protein (lipid:M1 molar ration 4:1) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Proteoliposomes composed of lipids from A/Puerto Rico/8/34 (H1N1) virus envelope together with the HA LI45 peptides loaded with M1 protein (lipid:M1 molar ration 4:1) monomer, 2000 kDa
Buffer: 100 mM NaCl, 50 mM MES buffer, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Nov 26
The Cytoplasmic Tail of Influenza A Virus Hemagglutinin and Membrane Lipid Composition Change the Mode of M1 Protein Association with the Lipid Bilayer Membranes 11(10):772 (2021)
...Konarev P, Fedorova N, Shtykova E, Ksenofontov A, Loshkarev N, Dadinova L, Timofeeva T, Abramchuk S, Moiseenko A, Baratova L, Svergun D, Batishchev O

SASDDM5 – Mutant mammalian prion protein mRNA (octo-repeat PrP mRNA) with KCl

octo-repeat PrP mRNA mutant experimental SAS data
DAMFILT model
Sample: octo-repeat PrP mRNA mutant dimer, 144 kDa human PrP ORF RNA
Buffer: 10 mM Tris buffer with 100 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Jun 6
Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes. Sci Rep 9(1):2465 (2019)
...Konarev PV, Goebel I, Svergun DI, Wills PR, Ignatova Z
RgGuinier 9.0 nm
Dmax 33.0 nm
VolumePorod 210 nm3

SASDLM5 – frataxin homolog, Yfh1, at 20 °C

Frataxin homolog, mitochondrial experimental SAS data
frataxin homolog, Yfh1, at 20 °C Rg histogram
Sample: Frataxin homolog, mitochondrial monomer, 14 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 20 mM HEPES, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Nov 28
The role of hydration in protein stability: comparison of the cold and heat unfolded states of Yfh1. J Mol Biol 417(5):413-24 (2012)
...Konarev PV, Svergun DI, Daura X, Temussi P, Pastore A
RgGuinier 2.1 nm

SASDAN5 – Cross-linked complex CytC_Adr

Cytochrome CAdrenodoxin experimental SAS data
DAMMIN model
Sample: Cytochrome C monomer, 11 kDa Escherichia coli protein
Adrenodoxin monomer, 11 kDa Escherichia coli protein
Buffer: 20 mM HEPES 2 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Jun 15
Dynamics in a pure encounter complex of two proteins studied by solution scattering and paramagnetic NMR spectroscopy. J Am Chem Soc 130(20):6395-403 (2008)
...Konarev PV, Svergun DI, Bernhardt R, Ubbink M
RgGuinier 2.1 nm
Dmax 8.5 nm
VolumePorod 42 nm3

SASDDN5 – Mutant mammalian prion protein mRNA (octo-repear PrP mRNA) with LiCl

octo-repeat PrP mRNA mutant experimental SAS data
DAMFILT model
Sample: octo-repeat PrP mRNA mutant dimer, 144 kDa human PrP ORF RNA
Buffer: 10 mM Tris buffer with 100 mM LiCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Jun 6
Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes. Sci Rep 9(1):2465 (2019)
...Konarev PV, Goebel I, Svergun DI, Wills PR, Ignatova Z
RgGuinier 8.9 nm
Dmax 33.0 nm
VolumePorod 223 nm3

SASDLN5 – frataxin homolog, Yfh1, at 50 °C

Frataxin homolog, mitochondrial experimental SAS data
frataxin homolog, Yfh1, at 50 °C Rg histogram
Sample: Frataxin homolog, mitochondrial monomer, 14 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 20 mM HEPES, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Nov 28
The role of hydration in protein stability: comparison of the cold and heat unfolded states of Yfh1. J Mol Biol 417(5):413-24 (2012)
...Konarev PV, Svergun DI, Daura X, Temussi P, Pastore A
RgGuinier 2.5 nm

SASDAP5 – Native complex CytC_Adr

Cytochrome C dimerAdrenodoxin dimer experimental SAS data
DAMMIN model
Sample: Cytochrome C dimer dimer, 22 kDa Escherichia coli protein
Adrenodoxin dimer dimer, 22 kDa Escherichia coli protein
Buffer: 20 mM HEPES 2 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Jun 15
Dynamics in a pure encounter complex of two proteins studied by solution scattering and paramagnetic NMR spectroscopy. J Am Chem Soc 130(20):6395-403 (2008)
...Konarev PV, Svergun DI, Bernhardt R, Ubbink M
RgGuinier 2.9 nm
Dmax 9.5 nm
VolumePorod 64 nm3

SASDDP5 – Mutant mammalian prion protein mRNA (octo-repear PrP mRNA) with KCl and pyridostatin (PDS)

octo-repeat PrP mRNA mutant experimental SAS data
DAMFILT model
Sample: octo-repeat PrP mRNA mutant dimer, 144 kDa human PrP ORF RNA
Buffer: 10 mM Tris buffer with 100 mM KCl and 1 mM PDS, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Jun 6
Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes. Sci Rep 9(1):2465 (2019)
...Konarev PV, Goebel I, Svergun DI, Wills PR, Ignatova Z
RgGuinier 9.2 nm
Dmax 33.0 nm
VolumePorod 260 nm3

SASDLP5 – Complex of the josephin domain of ataxin-3 with ubiquitin

Josephin domain of ataxin-3Polyubiquitin-B experimental SAS data
DAMMIF model
Sample: Josephin domain of ataxin-3 monomer, 21 kDa Homo sapiens protein
Polyubiquitin-B monomer, 9 kDa Homo sapiens protein
Buffer: 20 mM Na-phosphate, 2 mM DTT, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 7
Allosteric regulation of deubiquitylase activity through ubiquitination. Front Mol Biosci 2:2 (2015)
...Konarev PV, Svergun DI, Paulson HL, Pastore A
RgGuinier 2.1 nm
Dmax 6.5 nm
VolumePorod 45 nm3

SASDAQ5 – Lumazine Synthase

Lumazine Synthase experimental SAS data
DAMMIN model
Sample: Lumazine Synthase , 960 kDa Bacillus subtilis protein
Buffer: Borate buffer, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2004 Nov 25
Multiple assembly states of lumazine synthase: a model relating catalytic function and molecular assembly. J Mol Biol 362(4):753-70 (2006)
...Konarev PV, Petoukhov MV, Svergun DI, Xing L, Cheng RH, Haase I, Fischer M, Bacher A, Ladenstein R, Meining W
RgGuinier 6.2 nm
Dmax 15.5 nm
VolumePorod 1450 nm3

SASDLQ5 – Tricorn protease oligomers

Tricorn protease experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Tricorn protease hexamer, 730 kDa Thermoplasma acidophilum (strain … protein
Buffer: 20mM Tris-HCl, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2003 Jan 14
X-ray snapshots of peptide processing in mutants of tricorn-interacting factor F1 from Thermoplasma acidophilum. J Biol Chem 280(39):33387-96 (2005)
...Konarev PV, Svergun DI, Huber R, Kim JS
RgGuinier 5.9 nm

SASDAR5 – ProNGF

ProNGF experimental SAS data
DAMMIN model
Sample: ProNGF dimer, 45 kDa Mouse submandibulary glands protein
Buffer: 50 mM Naphosphat 0.5 M Ammonium Sulfate(NH4)2SO4, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Oct 25
Intrinsic structural disorder of mouse proNGF. Proteins 75(4):990-1009 (2009)
...Konarev PV, Gonfloni S, Malerba F, Schwarz E, Svergun DI, Cattaneo A, Lamba D
RgGuinier 2.6 nm
Dmax 8.0 nm
VolumePorod 92 nm3

SASDLR5 – Multidomain Regulatory Protein Rv1364c (monomer)

Multidomain regulatory protein Rv1364c experimental SAS data
GASBOR model
Sample: Multidomain regulatory protein Rv1364c monomer, 70 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 25 mM Tris-HCl, 50 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Feb 14
Structural characterization of the multidomain regulatory protein Rv1364c from Mycobacterium tuberculosis. Structure 19(1):56-69 (2011)
...Konarev PV, Panjikar S, Jordanova R, Svergun DI, Tucker PA
RgGuinier 3.8 nm
Dmax 14.0 nm
VolumePorod 130 nm3

SASDAS5 – ad11 Fab

aD11 Fab experimental SAS data
DAMMIN model
Sample: aD11 Fab dimer, 50 kDa Mus musculus protein
Buffer: 50 mM Na-phosphate 1mM ethylenediaminetetraacetic aci, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Oct 20
Dissecting NGF interactions with TrkA and p75 receptors by structural and functional studies of an anti-NGF neutralizing antibody. J Mol Biol 381(4):881-96 (2008)
...Konarev PV, Gonfloni S, Rudolph R, Svergun DI, Lamba D, Cattaneo A
RgGuinier 2.6 nm
Dmax 8.0 nm
VolumePorod 95 nm3

SASDLS5 – Multidomain Regulatory Protein Rv1364c (dimer)

Multidomain regulatory protein Rv1364c experimental SAS data
GASBOR model
Sample: Multidomain regulatory protein Rv1364c dimer, 139 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 25 mM Tris-HCl, 50 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Feb 14
Structural characterization of the multidomain regulatory protein Rv1364c from Mycobacterium tuberculosis. Structure 19(1):56-69 (2011)
...Konarev PV, Panjikar S, Jordanova R, Svergun DI, Tucker PA
RgGuinier 4.5 nm
Dmax 18.0 nm
VolumePorod 289 nm3

SASDAT5 – NGF

NGF experimental SAS data
DAMMIN model
Sample: NGF dimer, 50 kDa Mus musculus protein
Buffer: 10 mM Na-phosphate 150 mM NaCl, pH: 7.8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Oct 20
Dissecting NGF interactions with TrkA and p75 receptors by structural and functional studies of an anti-NGF neutralizing antibody. J Mol Biol 381(4):881-96 (2008)
...Konarev PV, Gonfloni S, Rudolph R, Svergun DI, Lamba D, Cattaneo A
RgGuinier 3.1 nm
Dmax 12.0 nm
VolumePorod 102 nm3

SASDLT5 – Modification methylase SsoII (M.SsoII) protein bound to 12-bp DNA

Modification methylase SsoII12-bp DNA experimental SAS data
Modification methylase SsoII (M.SsoII) protein bound to 12-bp DNA Rg histogram
Sample: Modification methylase SsoII monomer, 43 kDa Shigella sonnei protein
12-bp DNA monomer, 8 kDa DNA
Buffer: 50 mM Na-phosphate buffer, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Mar 13
Flexibility of the linker between the domains of DNA methyltransferase SsoII revealed by small-angle X-ray scattering: implications for transcription regulation in SsoII restriction-modification syste... PLoS One 9(4):e93453 (2014)
Konarev PV, Kachalova GS, Ryazanova AY, Kubareva EA, Karyagina AS, Bartunik HD, Svergun DI
RgGuinier 2.8 nm
Dmax 11.0 nm
VolumePorod 85 nm3