Browse by MODEL: Ab initio only

SASDWH7 – Wild type ferric binding protein (FbpA) in holo (with Fe) form in high ionic strength (HIS) buffer (PBS)

Iron-utilization periplasmic protein experimental SAS data
DAMFILT model
Sample: Iron-utilization periplasmic protein monomer, 34 kDa Haemophilus influenzae protein
Buffer: 10 mM Na2HPO4 . 7H2O 1.8 mM KH2PO4 137 mM NaCl 2.7 mM KCl 5% v/v Glycerol, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Aug 20
Conformational multiplicity of bacterial ferric binding protein revealed by small angle x-ray scattering and molecular dynamics calculations The Journal of Chemical Physics 158(8) (2023)
Liu G, Ekmen E, Jalalypour F, Mertens H, Jeffries C, Svergun D, Atilgan A, Atilgan C, Sayers Z
RgGuinier 2.0 nm
Dmax 6.2 nm
VolumePorod 34 nm3

SASDWJ7 – Wild type ferric binding protein (FbpA) in apo (no Fe) form in high ionic strength (HIS) buffer (PBS)

Iron-utilization periplasmic protein experimental SAS data
DAMFILT model
Sample: Iron-utilization periplasmic protein monomer, 34 kDa Haemophilus influenzae protein
Buffer: 10 mM Na2HPO4 . 7H2O 1.8 mM KH2PO4 137 mM NaCl 2.7 mM KCl 5% v/v Glycerol, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Dec 9
Conformational multiplicity of bacterial ferric binding protein revealed by small angle x-ray scattering and molecular dynamics calculations The Journal of Chemical Physics 158(8) (2023)
Liu G, Ekmen E, Jalalypour F, Mertens H, Jeffries C, Svergun D, Atilgan A, Atilgan C, Sayers Z
RgGuinier 2.1 nm
Dmax 6.5 nm
VolumePorod 39 nm3

SASDWK7 – D52A mutant of ferric binding protein (FbpA) in holo (with Fe) form in high ionic strength (HIS) buffer (PBS)

Iron-utilization periplasmic protein experimental SAS data
DAMMIN model
Sample: Iron-utilization periplasmic protein monomer, 34 kDa Haemophilus influenzae protein
Buffer: 10 mM Na2HPO4 . 7H2O 1.8 mM KH2PO4 137 mM NaCl 2.7 mM KCl 5% v/v Glycerol, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Dec 9
Conformational multiplicity of bacterial ferric binding protein revealed by small angle x-ray scattering and molecular dynamics calculations The Journal of Chemical Physics 158(8) (2023)
Liu G, Ekmen E, Jalalypour F, Mertens H, Jeffries C, Svergun D, Atilgan A, Atilgan C, Sayers Z
RgGuinier 2.0 nm
Dmax 5.9 nm
VolumePorod 33 nm3

SASDWL7 – D52A mutant of ferric binding protein (FbpA) in apo (no Fe) form in high ionic strength (HIS) buffer (PBS)

Iron-utilization periplasmic protein experimental SAS data
DAMMIN model
Sample: Iron-utilization periplasmic protein monomer, 34 kDa Haemophilus influenzae protein
Buffer: 10 mM Na2HPO4 . 7H2O 1.8 mM KH2PO4 137 mM NaCl 2.7 mM KCl 5% v/v Glycerol, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Sep 19
Conformational multiplicity of bacterial ferric binding protein revealed by small angle x-ray scattering and molecular dynamics calculations The Journal of Chemical Physics 158(8) (2023)
Liu G, Ekmen E, Jalalypour F, Mertens H, Jeffries C, Svergun D, Atilgan A, Atilgan C, Sayers Z
RgGuinier 2.1 nm
Dmax 6.2 nm
VolumePorod 40 nm3

SASDWM7 – D52A mutant of ferric binding protein (FbpA) in holo (with Fe) form in low ionic strength (LIS) buffer (1/10 PBS)

Iron-utilization periplasmic protein experimental SAS data
DAMFILT model
Sample: Iron-utilization periplasmic protein monomer, 34 kDa Haemophilus influenzae protein
Buffer: 1 mM Na2HPO4.7H2O, 0.18 mM KH2PO4, 13.7 mM NaCl, 0.27 mM KCl, 5%v/v Glycerol, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Aug 20
Conformational multiplicity of bacterial ferric binding protein revealed by small angle x-ray scattering and molecular dynamics calculations The Journal of Chemical Physics 158(8) (2023)
Liu G, Ekmen E, Jalalypour F, Mertens H, Jeffries C, Svergun D, Atilgan A, Atilgan C, Sayers Z
RgGuinier 2.0 nm
Dmax 6.1 nm
VolumePorod 24 nm3

SASDWN7 – Wild type ferric binding protein (FbpA) in apo (no Fe) form in low ionic strength (LIS) buffer (1/10 PBS)

Iron-utilization periplasmic protein experimental SAS data
DAMFILT model
Sample: Iron-utilization periplasmic protein monomer, 34 kDa Haemophilus influenzae protein
Buffer: 1 mM Na2HPO4.7H2O, 0.18 mM KH2PO4, 13.7 mM NaCl, 0.27 mM KCl, 5%v/v Glycerol, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Aug 20
Conformational multiplicity of bacterial ferric binding protein revealed by small angle x-ray scattering and molecular dynamics calculations The Journal of Chemical Physics 158(8) (2023)
Liu G, Ekmen E, Jalalypour F, Mertens H, Jeffries C, Svergun D, Atilgan A, Atilgan C, Sayers Z
RgGuinier 2.1 nm
Dmax 6.3 nm
VolumePorod 35 nm3

SASDWP7 – Wild type ferric binding protein (FbpA) in holo (with Fe) form in low ionic strength (LIS) buffer (1/10 PBS)

Iron-utilization periplasmic protein experimental SAS data
DAMMIN model
Sample: Iron-utilization periplasmic protein monomer, 34 kDa Haemophilus influenzae protein
Buffer: 1 mM Na2HPO4.7H2O, 0.18 mM KH2PO4, 13.7 mM NaCl, 0.27 mM KCl, 5%v/v Glycerol, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Aug 20
Conformational multiplicity of bacterial ferric binding protein revealed by small angle x-ray scattering and molecular dynamics calculations The Journal of Chemical Physics 158(8) (2023)
Liu G, Ekmen E, Jalalypour F, Mertens H, Jeffries C, Svergun D, Atilgan A, Atilgan C, Sayers Z
RgGuinier 2.0 nm
Dmax 6.1 nm
VolumePorod 29 nm3

SASDPX7 – DNA protection during starvation protein (Dps) loaded with FeSO4⋅7H2O in the amount corresponding to 50 iron atoms per dodecamer. Anomalous SAXS spanning the X-ray Fe-absorption edge 7.100-7.133 keV.

DNA protection during starvation protein experimental SAS data
DAMMIN model
Sample: DNA protection during starvation protein dodecamer, 224 kDa Escherichia coli (strain … protein
Buffer: 50 mM NaCl, 0.5 mM EDTA, 50 mM Tris-HCl, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Oct 5
An Anomalous Small-Angle X-Ray Scattering Study of the Formation of Iron Clusters in the Inner Cavity of the Ferritin-Like Protein Dps Moscow University Physics Bulletin 77(6):858-867 (2023)
Gordienko A, Mozhaev A, Gibizova V, Dadinova L
RgGuinier 3.8 nm
Dmax 14.0 nm
VolumePorod 32 nm3

SASDPY7 – DNA protection during starvation protein (Dps) loaded with FeSO4⋅7H2O in the amount corresponding to 500 iron atoms per dodecamer. Anomalous SAXS spanning the X-ray Fe-absorption edge 7.100-7.133 keV.

DNA protection during starvation protein experimental SAS data
DAMMIN model
Sample: DNA protection during starvation protein dodecamer, 224 kDa Escherichia coli (strain … protein
Buffer: 50 mM NaCl, 0.5 mM EDTA, 50 mM Tris-HCl, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Oct 5
An Anomalous Small-Angle X-Ray Scattering Study of the Formation of Iron Clusters in the Inner Cavity of the Ferritin-Like Protein Dps Moscow University Physics Bulletin 77(6):858-867 (2023)
Gordienko A, Mozhaev A, Gibizova V, Dadinova L
RgGuinier 7.4 nm
Dmax 12.0 nm

SASDPZ7 – DNA protection during starvation protein (Dps) loaded with FeSO4⋅7H2O in the amount corresponding to 2000 iron atoms per dodecamer. Anomalous SAXS spanning the X-ray Fe-absorption edge 7.100-7.133 keV.

DNA protection during starvation protein experimental SAS data
DAMMIN model
Sample: DNA protection during starvation protein dodecamer, 224 kDa Escherichia coli (strain … protein
Buffer: 50 mM NaCl, 0.5 mM EDTA, 50 mM Tris-HCl, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Oct 5
An Anomalous Small-Angle X-Ray Scattering Study of the Formation of Iron Clusters in the Inner Cavity of the Ferritin-Like Protein Dps Moscow University Physics Bulletin 77(6):858-867 (2023)
Gordienko A, Mozhaev A, Gibizova V, Dadinova L
RgGuinier 7.1 nm
Dmax 14.0 nm