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

SASDEL8 – Human Guanylate Binding Protein 1 (hGBP1), batch mode

human Guanylate-binding protein 1 experimental SAS data
PYMOL model
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 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 5.1 nm
Dmax 27.4 nm
VolumePorod 162 nm3

SASDEM8 – Human Guanylate Binding Protein 1 with GppNHp (hGBP1 + GppNHp), batch mode

human Guanylate-binding protein 1 experimental SAS data
PYMOL model
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 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 5.5 nm
Dmax 27.0 nm
VolumePorod 186 nm3

SASDF65 – Resistance to inhibitors of cholinesterase 8 homolog A (Ric8a) amino acids 1-492

Resistance to inhibitors of cholinesterase 8 homolog A experimental SAS data
BILBOMD model
Sample: Resistance to inhibitors of cholinesterase 8 homolog A monomer, 56 kDa Bos taurus protein
Buffer: 20 mM Tris, 150 mM KCl, 5 % glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Oct 27
Structural underpinnings of Ric8A function as a G-protein α-subunit chaperone and guanine-nucleotide exchange factor. Nat Commun 10(1):3084 (2019)
Srivastava D, Gakhar L, Artemyev NO
RgGuinier 3.4 nm
Dmax 12.7 nm
VolumePorod 88 nm3

4135 hits found.