Browse by MACROMOLECULE type: protein

SASDFF8 – Glutamine-binding periplasmic protein with hexahistidine tag (GlnBP), apo-form

Glutamine-binding periplasmic protein with hexahistidine tag experimental SAS data
Glutamine-binding periplasmic protein with hexahistidine tag Kratky plot
Sample: Glutamine-binding periplasmic protein with hexahistidine tag monomer, 26 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 2.1 nm
Dmax 6.2 nm
VolumePorod 35 nm3

SASDFG8 – Glutamine-binding periplasmic protein with hexahistidine tag (GlnBP) in the presence of glutamine - Gln-bound 10-fold excess

Glutamine-binding periplasmic protein with hexahistidine tag experimental SAS data
Glutamine-binding periplasmic protein with hexahistidine tag Kratky plot
Sample: Glutamine-binding periplasmic protein with hexahistidine tag monomer, 26 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 2.0 nm
Dmax 6.1 nm
VolumePorod 34 nm3

SASDFH8 – Glutamate/aspartate import solute-binding protein (DEBP), apo-form

Glutamate/aspartate import solute-binding protein experimental SAS data
Glutamate/aspartate import solute-binding protein Kratky plot
Sample: Glutamate/aspartate import solute-binding protein monomer, 32 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 2.3 nm
Dmax 8.5 nm
VolumePorod 44 nm3

SASDFJ8 – Glutamate/aspartate import solute-binding protein (DEBP) in the presence of glutamate - Glu-bound 10-fold excess

Glutamate/aspartate import solute-binding protein experimental SAS data
Glutamate/aspartate import solute-binding protein Kratky plot
Sample: Glutamate/aspartate import solute-binding protein monomer, 32 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 2.1 nm
Dmax 6.4 nm
VolumePorod 39 nm3

SASDEE8 – Farnesylated human Guanylate Binding Protein 1 (farn-hGBP1), monomer from SEC-SAXS

farnesylated human Guanylate-binding protein 1 experimental SAS data
Farnesylated human Guanylate Binding Protein 1 (farn-hGBP1), monomer from SEC-SAXS Rg histogram
Sample: Farnesylated human Guanylate-binding protein 1 monomer, 69 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 30
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 3.9 nm
Dmax 13.0 nm
VolumePorod 102 nm3

SASDEF8 – Human Guanylate Binding Protein 1 (hGBP1), monomer from SEC-SAXS

human Guanylate-binding protein 1 experimental SAS data
Human Guanylate Binding Protein 1 (hGBP1), monomer from SEC-SAXS Rg histogram
Sample: Human Guanylate-binding protein 1 monomer, 69 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 30
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 3.9 nm
Dmax 13.4 nm
VolumePorod 106 nm3

SASDEG8 – Human Guanylate Binding Protein 1 with GppNHp (hGBP1 + GppNHp), dimer from SEC-SAXS

human Guanylate-binding protein 1 experimental SAS data
Human Guanylate Binding Protein 1 with GppNHp (hGBP1 + GppNHp), dimer from SEC-SAXS Rg histogram
Sample: Human Guanylate-binding protein 1 dimer, 138 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, 0.2 mM GppNHp, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 30
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 5.5 nm
Dmax 22.0 nm
VolumePorod 270 nm3

SASDEH8 – Human Guanylate Binding Protein 1 with GppNHp (hGBP1 + GppNHp), monomer from SEC-SAXS

human Guanylate-binding protein 1 experimental SAS data
Human Guanylate Binding Protein 1 with GppNHp (hGBP1 + GppNHp), monomer from SEC-SAXS Rg histogram
Sample: Human Guanylate-binding protein 1 monomer, 69 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, 0.2 mM GppNHp, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 30
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 4.5 nm
Dmax 20.5 nm
VolumePorod 120 nm3

SASDEJ8 – Human Guanylate Binding Protein 1 (hGBP1), dimer from SEC-SAXS

human Guanylate-binding protein 1 experimental SAS data
Human Guanylate Binding Protein 1 (hGBP1), dimer from SEC-SAXS Rg histogram
Sample: Human Guanylate-binding protein 1 dimer, 138 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 30
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 4.8 nm
Dmax 15.6 nm
VolumePorod 211 nm3

SASDEK8 – Farnesylated human Guanylate Binding Protein 1 (farn-hGBP1), batch mode

farnesylated human Guanylate-binding protein 1 experimental SAS data
PYMOL model
Sample: Farnesylated human Guanylate-binding protein 1 monomer, 69 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2016 May 8
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 3.8 nm
Dmax 14.3 nm
VolumePorod 102 nm3