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130 hits found for Petr Konarev

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

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

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

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

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

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

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

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

SASDAU5 – ad11 Fab + NGF

aD11 FabNGF experimental SAS data
DAMMIN model
Sample: aD11 Fab dimer, 50 kDa Mus musculus protein
NGF dimer, 50 kDa Mus musculus protein
Buffer: 30 mM Na-phosphate 75 mM NaCl, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Dec 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 4.3 nm
Dmax 16.0 nm
VolumePorod 255 nm3

SASDLU5 – Complex formed between the replication origin-binding protein UL9 (C-terminal domains) with 15-bp DNA

Replication origin-binding protein15-bp DNA experimental SAS data
MONSA model
Sample: Replication origin-binding protein dimer, 81 kDa Human herpesvirus 1 … protein
15-bp DNA monomer, 9 kDa DNA
Buffer: 20 mM Tris-HCl, 50 mM NaCl, 5 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 May 27
Structural and biophysical characterization of the proteins interacting with the herpes simplex virus 1 origin of replication. J Biol Chem 284(24):16343-16353 (2009)
...Konarev P, Makhov AM, Fullerton SW, Sinz A, Kalkhof S, McGeehan JE, Cary PD, Griffith JD, Svergun D, Kneale GG, Tucker PA
RgGuinier 3.6 nm
Dmax 15.0 nm

SASDAV5 – apo XMRV RT

apo XMRV RT experimental SAS data
CRYSOL model
Sample: apo XMRV RT monomer, 75 kDa Escherichia coli protein
Buffer: 10 mM HEPES 100 mM KCl 5% Glycerol, pH: 6.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Dec 8
Structural analysis of monomeric retroviral reverse transcriptase in complex with an RNA/DNA hybrid. Nucleic Acids Res 41(6):3874-87 (2013)
...Konarev PV, Rausch JW, Bona MK, Svergun DI, Bujnicki JM, Le Grice SF, Nowotny M
RgGuinier 4.0 nm
Dmax 13.5 nm
VolumePorod 160 nm3

SASDLV5 – Myosin Filament-Linking Protein Myomesin-1 (domains My9-My13, dimer)

Myomesin-1 experimental SAS data
DAMMIN model
Sample: Myomesin-1 dimer, 121 kDa Homo sapiens protein
Buffer: 25 mMTris-HCl, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 May 10
Superhelical architecture of the myosin filament-linking protein myomesin with unusual elastic properties. PLoS Biol 10(2):e1001261 (2012)
...Konarev PV, Svergun DI, Morris E, Rief M, Wilmanns M
RgGuinier 9.6 nm
Dmax 37.0 nm

SASDAW5 – XMRV RT + DNA/RNA hybrid

apo XMRV RTRNA_DNA hybrid substrate experimental SAS data
CRYSOL model
Sample: apo XMRV RT monomer, 75 kDa Escherichia coli protein
RNA_DNA hybrid substrate monomer, 15 kDa
Buffer: 10 mM HEPES 100 mM KCl 5% Glycerol, pH: 6.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Dec 8
Structural analysis of monomeric retroviral reverse transcriptase in complex with an RNA/DNA hybrid. Nucleic Acids Res 41(6):3874-87 (2013)
...Konarev PV, Rausch JW, Bona MK, Svergun DI, Bujnicki JM, Le Grice SF, Nowotny M
RgGuinier 3.5 nm
Dmax 11.5 nm
VolumePorod 155 nm3

SASDLW5 – Cytochrome c nitrite reductase from Thioalkalivibrio nitratireducens

Cytochrome c-552 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Cytochrome c-552 hexamer, 356 kDa Thioalkalivibrio nitratireducens (strain … protein
Buffer: Tris-borate buffer, pH: 8.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 May 8
Isolation and oligomeric composition of cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio nitratireducens. Biochemistry (Mosc) 73(2):164-70 (2008)
...Konarev PV, Polyakov KM, Svergun DI, Trofimov AA, Khomenkov VG, Zvyagilskaya RA, Popov VO
RgGuinier 4.8 nm

SASDAV6 – Cysteine desulfurase IscS dimer

Cysteine desulfurase IscS experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Cysteine desulfurase IscS dimer, 87 kDa Escherichia coli protein
Buffer: 20 mM Tris-HCl 150 mM NaCl 10 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5
Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Nat Commun 1:95 (2010)
...Konarev PV, Iannuzzi C, Pastore C, Adinolfi S, Martin SR, Svergun DI, Pastore A
RgGuinier 3.2 nm
Dmax 10.9 nm

SASDAW6 – Iron-sulfur cluster assembly scaffold IscU monomer

Iron-sulfur cluster assembly scaffold protein IscU experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Iron-sulfur cluster assembly scaffold protein IscU monomer, 14 kDa Escherichia coli protein
Buffer: 20 mM Tris-HCl 150 mM NaCl 10 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5
Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Nat Commun 1:95 (2010)
...Konarev PV, Iannuzzi C, Pastore C, Adinolfi S, Martin SR, Svergun DI, Pastore A
RgGuinier 1.9 nm
Dmax 6.4 nm

SASDAX6 – Protein CyaY monomer

Protein CyaY experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Protein CyaY monomer, 12 kDa Escherichia coli protein
Buffer: 20 mM Tris-HCl 150 mM NaCl 10 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5
Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Nat Commun 1:95 (2010)
...Konarev PV, Iannuzzi C, Pastore C, Adinolfi S, Martin SR, Svergun DI, Pastore A
RgGuinier 1.5 nm
Dmax 5.0 nm

SASDAY6 – IcsS-dimer and IscU-dimer complex

Cysteine desulfurase IscSIron-sulfur cluster assembly scaffold protein IscU experimental SAS data
DAMMIF model
Sample: Cysteine desulfurase IscS dimer, 87 kDa Escherichia coli protein
Iron-sulfur cluster assembly scaffold protein IscU dimer, 29 kDa Escherichia coli protein
Buffer: 20 mM Tris-HCl 150 mM NaCl 10 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5
Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Nat Commun 1:95 (2010)
...Konarev PV, Iannuzzi C, Pastore C, Adinolfi S, Martin SR, Svergun DI, Pastore A
RgGuinier 3.6 nm
Dmax 12.1 nm

SASDAZ6 – CyaY-dimer and IscS-dimer complex

Cysteine desulfurase IscSProtein CyaY experimental SAS data
SASREF model
Sample: Cysteine desulfurase IscS dimer, 87 kDa Escherichia coli protein
Protein CyaY dimer, 24 kDa Escherichia coli protein
Buffer: 20 mM Tris-HCl, 50 mM NaCl, 10 mM β-mercaptoethanol and ferrous ammonium sulphate, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5
Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Nat Commun 1:95 (2010)
...Konarev PV, Iannuzzi C, Pastore C, Adinolfi S, Martin SR, Svergun DI, Pastore A
RgGuinier 3.1 nm
Dmax 10.9 nm

SASDA27 – IcsS, IscU and CyaY dimeric complex

Cysteine desulfurase IscSIron-sulfur cluster assembly scaffold protein IscUProtein CyaY experimental SAS data
SASREF model
Sample: Cysteine desulfurase IscS dimer, 87 kDa Escherichia coli protein
Iron-sulfur cluster assembly scaffold protein IscU dimer, 29 kDa Escherichia coli protein
Protein CyaY dimer, 24 kDa Escherichia coli protein
Buffer: 20 mM Tris-HCl 150 mM NaCl 10 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5
Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Nat Commun 1:95 (2010)
...Konarev PV, Iannuzzi C, Pastore C, Adinolfi S, Martin SR, Svergun DI, Pastore A
RgGuinier 3.5 nm
Dmax 11.9 nm

SASDJ47 – Polyglutamine protein ataxin-3 (Q13)

Ataxin-3 (polyglutamine protein ataxin-3 (Q13)) experimental SAS data
Polyglutamine protein ataxin-3 (Q13) Rg histogram
Sample: Ataxin-3 (polyglutamine protein ataxin-3 (Q13)) monomer, 41 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate buffer, 2 mM TCEP, 5% glycerol, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 May 24
Capturing the Conformational Ensemble of the Mixed Folded Polyglutamine Protein Ataxin-3. Structure (2020)
...Konarev PV, Svergun DI, Pastore A
RgGuinier 4.0 nm
Dmax 14.1 nm
VolumePorod 79 nm3

SASDL47 – Oligomeric composition of AXH Domain of Ataxin-1 (wild type and A567G, I580A mutants)

Ataxin-1 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Ataxin-1 monomer, 14 kDa Homo sapiens protein
Buffer: 20 mM Tris-HCl, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Oct 21
Self-assembly and conformational heterogeneity of the AXH domain of ataxin-1: an unusual example of a chameleon fold. Biophys J 104(6):1304-13 (2013)
...Konarev PV, Svergun DI, Martin SR, Chen YW, Pastore A
RgGuinier 5.5 nm

SASDJ57 – Polyglutamine protein ataxin-3 (Q54)

Ataxin-3 (polyglutamine protein ataxin-3 (Q54)) experimental SAS data
Polyglutamine protein ataxin-3 (Q54) Rg histogram
Sample: Ataxin-3 (polyglutamine protein ataxin-3 (Q54)) monomer, 46 kDa protein
Buffer: 20 mM sodium phosphate buffer, 2 mM TCEP, 5% glycerol, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 May 24
Capturing the Conformational Ensemble of the Mixed Folded Polyglutamine Protein Ataxin-3. Structure (2020)
...Konarev PV, Svergun DI, Pastore A
RgGuinier 4.2 nm
Dmax 15.5 nm
VolumePorod 89 nm3