Browse by DISSEMINATION: Published

SASDWG7 – D52A mutant of 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 28 nm3

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

SASDPB6 – Fibronectin 2 and 3 of cell adhesion molecule L1 (L1CAM) expressed in HEK293S GnTI-

Neural cell adhesion molecule L1 experimental SAS data
DAMMIN model
Sample: Neural cell adhesion molecule L1 monomer, 24 kDa Homo sapiens protein
Buffer: 50 mM MES pH 6.5, 150 mM NaCl, 5% glycerol, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 May 11
X‐ray structure and function of fibronectin domains two and three of the neural cell adhesion molecule L1 The FASEB Journal 37(3) (2023)
Guédez G, Loers G, Jeffries C, Kozak S, Meijers R, Svergun D, Schachner M, Löw C
RgGuinier 2.8 nm
Dmax 9.5 nm
VolumePorod 68 nm3

SASDPC6 – Fibronectin 2 and 3 of cell adhesion molecule L1 (L1CAM) expressed in HEK293F

Neural cell adhesion molecule L1 experimental SAS data
DAMMIN model
Sample: Neural cell adhesion molecule L1 monomer, 24 kDa Homo sapiens protein
Buffer: 50 mM MES pH 6.5, 150 mM NaCl, 5% glycerol, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 May 11
X‐ray structure and function of fibronectin domains two and three of the neural cell adhesion molecule L1 The FASEB Journal 37(3) (2023)
Guédez G, Loers G, Jeffries C, Kozak S, Meijers R, Svergun D, Schachner M, Löw C
RgGuinier 2.9 nm
Dmax 9.9 nm
VolumePorod 72 nm3