Browse by MODEL: Ab initio only

SASDND6 – Human ganglioside-induced differentiation-associated protein 1 (GDAP1) missense mutant H123R, construct GDAP1∆302-358

Ganglioside-induced differentiation-associated protein 1 (H123R) experimental SAS data
GASBOR model
Sample: Ganglioside-induced differentiation-associated protein 1 (H123R) dimer, 70 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Oct 8
Structural insights into Charcot-Marie-Tooth disease-linked mutations in human GDAP1. FEBS Open Bio (2022)
Sutinen A, Nguyen GTT, Raasakka A, Muruganandam G, Loris R, Ylikallio E, Tyynismaa H, Bartesaghi L, Ruskamo S, Kursula P
RgGuinier 3.1 nm
Dmax 9.9 nm
VolumePorod 107 nm3

SASDNE6 – Human ganglioside-induced differentiation-associated protein 1 (GDAP1) missense mutant R120W, construct GDAP1∆302-358

Ganglioside-induced differentiation-associated protein 1 (R120W) experimental SAS data
GASBOR model
Sample: Ganglioside-induced differentiation-associated protein 1 (R120W) dimer, 70 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Jul 1
Structural insights into Charcot-Marie-Tooth disease-linked mutations in human GDAP1. FEBS Open Bio (2022)
Sutinen A, Nguyen GTT, Raasakka A, Muruganandam G, Loris R, Ylikallio E, Tyynismaa H, Bartesaghi L, Ruskamo S, Kursula P
RgGuinier 3.1 nm
Dmax 10.0 nm
VolumePorod 105 nm3

SASDNY7 – DNA-binding protein from starved cells: DgrDpsWT in 50 mM MOPS, 50 mM NaCl pH 7.0

DNA protection during starvation, DPS (Ferritin superfamily) experimental SAS data
GASBOR model
Sample: DNA protection during starvation, DPS (Ferritin superfamily) dodecamer, 270 kDa Deinococcus grandis protein
Buffer: 50 mM MOPS-NaOH, 50 mM NaCl, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Oct 22
The Conformation of the N-Terminal Tails of Deinococcus grandis Dps Is Modulated by the Ionic Strength International Journal of Molecular Sciences 23(9):4871 (2022)
Guerra J, Blanchet C, Vieira B, Almeida A, Waerenborgh J, Jones N, Hoffmann S, Tavares P, Pereira A
RgGuinier 4.4 nm
Dmax 16.1 nm
VolumePorod 409 nm3

SASDNZ7 – DNA-binding protein from starved cells: DgrDpsWT in 50 mM MOPS, 80 mM NaCl pH 7.0

DNA protection during starvation, DPS (Ferritin superfamily) experimental SAS data
GASBOR model
Sample: DNA protection during starvation, DPS (Ferritin superfamily) dodecamer, 270 kDa Deinococcus grandis protein
Buffer: 50 mM MOPS-NaOH, 80 mM NaCl, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Oct 22
The Conformation of the N-Terminal Tails of Deinococcus grandis Dps Is Modulated by the Ionic Strength International Journal of Molecular Sciences 23(9):4871 (2022)
Guerra J, Blanchet C, Vieira B, Almeida A, Waerenborgh J, Jones N, Hoffmann S, Tavares P, Pereira A
RgGuinier 4.5 nm
Dmax 17.1 nm
VolumePorod 475 nm3

SASDN28 – DNA-binding protein from starved cells: DgrDpsWT in 50 mM MOPS, 230 mM NaCl pH 7.0

DNA protection during starvation, DPS (Ferritin superfamily) experimental SAS data
GASBOR model
Sample: DNA protection during starvation, DPS (Ferritin superfamily) dodecamer, 270 kDa Deinococcus grandis protein
Buffer: 50 mM MOPS-NaOH, 230 mM NaCl, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Oct 22
The Conformation of the N-Terminal Tails of Deinococcus grandis Dps Is Modulated by the Ionic Strength International Journal of Molecular Sciences 23(9):4871 (2022)
Guerra J, Blanchet C, Vieira B, Almeida A, Waerenborgh J, Jones N, Hoffmann S, Tavares P, Pereira A
RgGuinier 4.5 nm
Dmax 20.6 nm
VolumePorod 438 nm3

SASDN38 – DNA-binding protein from starved cells: DgrDpsWT in 50 mM MOPS, 480 mM NaCl pH 7.0

DNA protection during starvation, DPS (Ferritin superfamily) experimental SAS data
GASBOR model
Sample: DNA protection during starvation, DPS (Ferritin superfamily) dodecamer, 270 kDa Deinococcus grandis protein
Buffer: 50 mM MOPS-NaOH, 480 mM NaCl, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Oct 22
The Conformation of the N-Terminal Tails of Deinococcus grandis Dps Is Modulated by the Ionic Strength International Journal of Molecular Sciences 23(9):4871 (2022)
Guerra J, Blanchet C, Vieira B, Almeida A, Waerenborgh J, Jones N, Hoffmann S, Tavares P, Pereira A
RgGuinier 4.8 nm
Dmax 20.5 nm
VolumePorod 430 nm3

SASDN48 – DNA-binding protein from starved cells (tailless): DgrDps∆N in 50 mM MOPS, 50 mM NaCl pH 7.0

DNA protection during starvation, DPS-∆N (Ferritin superfamily) experimental SAS data
DAMMIN model
Sample: DNA protection during starvation, DPS-∆N (Ferritin superfamily) dodecamer, 218 kDa Deinococcus grandis protein
Buffer: 50 mM MOPS-NaOH, 50 mM NaCl, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Oct 22
The Conformation of the N-Terminal Tails of Deinococcus grandis Dps Is Modulated by the Ionic Strength International Journal of Molecular Sciences 23(9):4871 (2022)
Guerra J, Blanchet C, Vieira B, Almeida A, Waerenborgh J, Jones N, Hoffmann S, Tavares P, Pereira A
RgGuinier 3.8 nm
Dmax 9.3 nm
VolumePorod 290 nm3

SASDN58 – DNA-binding protein from starved cells (tailless): DgrDps∆N in 50 mM MOPS, 230 mM NaCl pH 7.0

DNA protection during starvation, DPS-∆N (Ferritin superfamily) experimental SAS data
DAMMIN model
Sample: DNA protection during starvation, DPS-∆N (Ferritin superfamily) dodecamer, 218 kDa Deinococcus grandis protein
Buffer: 50 mM MOPS-NaOH, 230 mM NaCl, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Oct 22
The Conformation of the N-Terminal Tails of Deinococcus grandis Dps Is Modulated by the Ionic Strength International Journal of Molecular Sciences 23(9):4871 (2022)
Guerra J, Blanchet C, Vieira B, Almeida A, Waerenborgh J, Jones N, Hoffmann S, Tavares P, Pereira A
RgGuinier 3.8 nm
Dmax 8.8 nm
VolumePorod 291 nm3

SASDML8 – Sulfite reductase hemoprotein

Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) experimental SAS data
Sample: Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) monomer, 64 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at EQ-SANS (BL-6), Spallation Neutron Source on 2018 Jul 13
Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase. Biophys J (2022)
Murray DT, Walia N, Weiss KL, Stanley CB, Randolph PS, Nagy G, Stroupe ME
RgGuinier 2.3 nm
Dmax 7.2 nm
VolumePorod 71 nm3

SASDMM8 – Reconstituted sulfite reductase dodecamer with partially deuterated hemoprotein in 0% D2O

Sulfite reductase [NADPH] hemoprotein beta-componentSulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) experimental SAS data
Sample: Sulfite reductase [NADPH] hemoprotein beta-component tetramer, 256 kDa Escherichia coli (strain … protein
Sulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) octamer, 565 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at EQ-SANS (BL-6), Spallation Neutron Source on 2021 Apr 3
Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase. Biophys J (2022)
Murray DT, Walia N, Weiss KL, Stanley CB, Randolph PS, Nagy G, Stroupe ME
RgGuinier 11.2 nm
Dmax 30.5 nm