SASDF76 – Polyphosphate-targeting protein A

Polyphosphate-targeting protein A experimental SAS data
CORAL model
Sample: Polyphosphate-targeting protein A dimer, 79 kDa Streptomyces chartreusis protein
Buffer: 20 mM Tris-HCl 400 mM NaCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Nov 24
Structural and biochemical analysis of a phosin from Streptomyces chartreusis reveals a combined polyphosphate- and metal-binding fold. FEBS Lett (2019)
Werten S, Rustmeier NH, Gemmer M, Virolle MJ, Hinrichs W
RgGuinier 3.5 nm
Dmax 11.8 nm
VolumePorod 124 nm3

SASDFK3 – Splicing factor, proline- and glutamine-rich (SFPQ)

Splicing factor, proline- and glutamine-rich experimental SAS data
CORAL model
Sample: Splicing factor, proline- and glutamine-rich dimer, 60 kDa Homo sapiens protein
Buffer: 20 mM Tris-HCl, 250 mM NaCl, 5% (v/v) glycerol, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Apr 19
A new crystal structure and small-angle X-ray scattering analysis of the homodimer of human SFPQ. Acta Crystallogr F Struct Biol Commun 75(Pt 6):439-449 (2019)
Hewage TW, Caria S, Lee M
RgGuinier 2.8 nm
Dmax 8.2 nm
VolumePorod 91 nm3

SASDKD4 – In vitro DNA protection during starvation protein (Dps)/DNA co-crystallization

DNA protection during starvation protein experimental SAS data
DNA protection during starvation protein Kratky plot
Sample: DNA protection during starvation protein dodecamer, 224 kDa Escherichia coli (strain … protein
Buffer: 50 mM Tris-HCl, 50 mM NaCl, 0.5 mM EDTA, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Nov 27
Protective Dps-DNA co-crystallization in stressed cells: an in vitro structural study by small-angle X-ray scattering and cryo-electron tomography. FEBS Lett 593(12):1360-1371 (2019)
Dadinova LA, Chesnokov YM, Kamyshinsky RA, Orlov IA, Petoukhov MV, Mozhaev AA, Soshinskaya EY, Lazarev VN, Manuvera VA, Orekhov AS, Vasiliev AL, Shtykova EV

SASDF86 – Human Galectin-10 (Tyr69Glu mutant)

Galectin-10 Tyr69Glu experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Galectin-10 Tyr69Glu dimer, 33 kDa Homo sapiens protein
Buffer: 20 mM Hepes 150 NaCl, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2018 Feb 4
Protein crystallization promotes type 2 immunity and is reversible by antibody treatment. Science 364(6442) (2019)
Persson EK, Verstraete K, Heyndrickx I, Gevaert E, Aegerter H, Percier JM, Deswarte K, Verschueren KHG, Dansercoer A, Gras D, Chanez P, Bachert C, Gonçalves A, Van Gorp H, De Haard H, Blanchetot C, Sa...
RgGuinier 2.1 nm
Dmax 8.2 nm
VolumePorod 46 nm3

SASDF34 – Free Nuclear receptor CoRepressor NID (spanning from residue Gln2059 to Glu2325)

Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID) experimental SAS data
Sample: Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID) monomer, 29 kDa Mus musculus protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Jun 20
Interplay of Protein Disorder in Retinoic Acid Receptor Heterodimer and Its Corepressor Regulates Gene Expression. Structure (2019)
Cordeiro TN, Sibille N, Germain P, Barthe P, Boulahtouf A, Allemand F, Bailly R, Vivat V, Ebel C, Barducci A, Bourguet W, le Maire A, Bernadó P
RgGuinier 4.7 nm
Dmax 17.7 nm
VolumePorod 102 nm3

SASDF44 – RXR/RAR Heterodimer : N-CoRNID Complex (1:1)

Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID)Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD)Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB) experimental SAS data
Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID) Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD) Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB) Kratky plot
Sample: Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID) monomer, 29 kDa Mus musculus protein
Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD) monomer, 26 kDa Mus musculus protein
Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB) monomer, 28 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Jul 23
Interplay of Protein Disorder in Retinoic Acid Receptor Heterodimer and Its Corepressor Regulates Gene Expression. Structure (2019)
Cordeiro TN, Sibille N, Germain P, Barthe P, Boulahtouf A, Allemand F, Bailly R, Vivat V, Ebel C, Barducci A, Bourguet W, le Maire A, Bernadó P
RgGuinier 4.8 nm
Dmax 19.4 nm
VolumePorod 167 nm3

SASDF54 – RXRΔH12/RAR Heterodimer : N-CoRNID Complex (1:1)

Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID)Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD)Retinoid-X receptor alpha (RXR-alpha) Δ helix12 experimental SAS data
Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID) Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD) Retinoid-X receptor alpha (RXR-alpha) Δ helix12 Kratky plot
Sample: Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID) monomer, 29 kDa Mus musculus protein
Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD) monomer, 26 kDa Mus musculus protein
Retinoid-X receptor alpha (RXR-alpha) Δ helix12 monomer, 24 kDa Mus musculus protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Jul 23
Interplay of Protein Disorder in Retinoic Acid Receptor Heterodimer and Its Corepressor Regulates Gene Expression. Structure (2019)
Cordeiro TN, Sibille N, Germain P, Barthe P, Boulahtouf A, Allemand F, Bailly R, Vivat V, Ebel C, Barducci A, Bourguet W, le Maire A, Bernadó P
RgGuinier 4.2 nm
Dmax 15.7 nm
VolumePorod 183 nm3

SASDF64 – RXR/RAR Heterodimer : N-CoRNID Complex (1:1) with RAR inverse agonist (BMS493)

Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID)Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD)Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB) experimental SAS data
Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID) Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD) Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB) Kratky plot
Sample: Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID) monomer, 29 kDa Mus musculus protein
Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD) monomer, 26 kDa Mus musculus protein
Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB) monomer, 28 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Jul 23
Interplay of Protein Disorder in Retinoic Acid Receptor Heterodimer and Its Corepressor Regulates Gene Expression. Structure (2019)
Cordeiro TN, Sibille N, Germain P, Barthe P, Boulahtouf A, Allemand F, Bailly R, Vivat V, Ebel C, Barducci A, Bourguet W, le Maire A, Bernadó P
RgGuinier 4.8 nm
Dmax 19.5 nm
VolumePorod 178 nm3

SASDF74 – RXR/RARI396E Heterodimer : N-CoRNID Complex (1:1)

Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID)Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD)Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB) mutant I396E experimental SAS data
Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID) Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD) Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB) mutant I396E Kratky plot
Sample: Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID) monomer, 29 kDa Mus musculus protein
Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD) monomer, 26 kDa Mus musculus protein
Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB) mutant I396E monomer, 28 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2015 Mar 9
Interplay of Protein Disorder in Retinoic Acid Receptor Heterodimer and Its Corepressor Regulates Gene Expression. Structure (2019)
Cordeiro TN, Sibille N, Germain P, Barthe P, Boulahtouf A, Allemand F, Bailly R, Vivat V, Ebel C, Barducci A, Bourguet W, le Maire A, Bernadó P
RgGuinier 5.3 nm
Dmax 22.4 nm
VolumePorod 171 nm3

SASDF84 – RXR/RAR Heterodimer : N-CoRNID Complex (1:1) with RAR agonist (Am580)

Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID)Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD)Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB) experimental SAS data
Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID) Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD) Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB) Kratky plot
Sample: Nuclear receptor CoRepressor 1; Nuclear Receptor Interaction Domain (NID) monomer, 29 kDa Mus musculus protein
Retinoid-X receptor alpha (RXR-alpha) Ligand Binding Domain (LBD) monomer, 26 kDa Mus musculus protein
Retinoic acid receptor alpha (RAR-alpha) Ligand binding domain (LDB) monomer, 28 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Jul 23
Interplay of Protein Disorder in Retinoic Acid Receptor Heterodimer and Its Corepressor Regulates Gene Expression. Structure (2019)
Cordeiro TN, Sibille N, Germain P, Barthe P, Boulahtouf A, Allemand F, Bailly R, Vivat V, Ebel C, Barducci A, Bourguet W, le Maire A, Bernadó P
RgGuinier 4.2 nm
Dmax 17.2 nm
VolumePorod 131 nm3

4725 hits found.