Browse by MODEL: Ab initio only

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)
Zanchi D, 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)
Zanchi D, 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)
Zanchi D, 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)
Zanchi D, 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)
Zanchi D, Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 1.2 nm
Dmax 3.6 nm

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)
Manolaridis I, Mumtsidu E, 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

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)
Werner A, 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)
Werner A, 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)
Werner A, Konarev PV, Svergun DI, Hahn U
RgGuinier 2.3 nm
Dmax 8.0 nm
VolumePorod 24 nm3

SASDMC7 – Nuclear fragile X mental retardation-interacting protein 2 (FRMP)

Nuclear fragile X mental retardation-interacting protein 2 experimental SAS data
DAMMIN model
Sample: Nuclear fragile X mental retardation-interacting protein 2 monomer, 59 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl pH 8.0, 5 mM TCEP, pH:
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Oct 11
A study of the ultrastructure of fragile-X-related proteins. Biochem J 419(2):347-57 (2009)
Sjekloća L, Konarev PV, Eccleston J, Taylor IA, Svergun DI, Pastore A
RgGuinier 4.1 nm
Dmax 15.0 nm
VolumePorod 92 nm3