Browse by MODEL: Ensemble

SASDG34 – Subgenomic flavivirus RNAs from West nile virus

Subgenomic flavivirus RNAs from West nile virus experimental SAS data
Subgenomic flavivirus RNAs from West nile virus Rg histogram
Sample: Subgenomic flavivirus RNAs from West nile virus monomer, 170 kDa West Nile virus RNA
Buffer: 20mM Tris-HCl, 100mM NaCl, 5mM MgCl2, pH: 7.5
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2017 Mar 13
Long non-coding subgenomic flavivirus RNAs have extended 3D structures and are flexible in solution. EMBO Rep 20(11):e47016 (2019)
Zhang Y, Zhang Y, Liu ZY, Cheng ML, Ma J, Wang Y, Qin CF, Fang X
RgGuinier 7.9 nm
Dmax 31.8 nm
VolumePorod 261 nm3

SASDGZ3 – Subgenomic flavivirus RNAs from Zika virus

Subgenomic flavivirus RNA from Zika virus experimental SAS data
Subgenomic flavivirus RNAs from Zika virus Rg histogram
Sample: Subgenomic flavivirus RNA from Zika virus monomer, 133 kDa Zika virus RNA
Buffer: 20mM Tris-HCl, 100mM NaCl, 5mM MgCl2, pH: 7.5
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2017 Mar 13
Long non-coding subgenomic flavivirus RNAs have extended 3D structures and are flexible in solution. EMBO Rep 20(11):e47016 (2019)
Zhang Y, Zhang Y, Liu ZY, Cheng ML, Ma J, Wang Y, Qin CF, Fang X
RgGuinier 7.5 nm
Dmax 29.6 nm
VolumePorod 230 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

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

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

SASDF52 – dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE

Dosage compensation regulator experimental SAS data
dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE Rg histogram
Sample: Dosage compensation regulator monomer, 29 kDa Drosophila melanogaster protein
Buffer: 20 mM NaPO4, 200 mM NaCl, 1 mM DTT, pH: 6.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 29
Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless. Nucleic Acids Res 47(8):4319-4333 (2019)
Ankush Jagtap PK, Müller M, Masiewicz P, von Bülow S, Hollmann NM, Chen PC, Simon B, Thomae AW, Becker PB, Hennig J
RgGuinier 3.2 nm
Dmax 12.5 nm
VolumePorod 22 nm3

SASDET6 – Polyglutamine-binding protein 1 p.Lys192Serfs*7 (PQBP-1 XLID mutant K192Sfs*7)

Polyglutamine-binding protein 1 p.Lys192Serfs*7 experimental SAS data
Polyglutamine-binding protein 1 p.Lys192Serfs*7 (PQBP-1 XLID mutant K192Sfs*7) Rg histogram
Sample: Polyglutamine-binding protein 1 p.Lys192Serfs*7 dimer, 47 kDa Homo sapiens protein
Buffer: Phosphate-buffered saline, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2013 Feb 15
Frameshift PQBP-1 mutants K192Sfs*7 and R153Sfs*41 implicated in X-linked intellectual disability form stable dimers. J Struct Biol (2019)
Rahman SK, Okazawa H, Chen YW
RgGuinier 3.5 nm
Dmax 13.0 nm
VolumePorod 114 nm3

SASDEU6 – Polyglutamine-binding protein 1 p.Arg153Serfs*41 (PQBP-1 XLID mutant R153Sfs*41)

Polyglutamine-binding protein 1 p.Arg153Serfs*41 experimental SAS data
Polyglutamine-binding protein 1 p.Arg153Serfs*41 (PQBP-1 XLID mutant R153Sfs*41) Rg histogram
Sample: Polyglutamine-binding protein 1 p.Arg153Serfs*41 dimer, 44 kDa Homo sapiens protein
Buffer: Phosphate-buffered saline, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2013 Feb 15
Frameshift PQBP-1 mutants K192Sfs*7 and R153Sfs*41 implicated in X-linked intellectual disability form stable dimers. J Struct Biol (2019)
Rahman SK, Okazawa H, Chen YW
RgGuinier 3.6 nm
Dmax 13.0 nm
VolumePorod 100 nm3