Browse by MODEL: No model

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

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

SASDFA5 – Unposphorylated Resistance to inhibitors of cholinesterase 8 homolog A, Ric-8A, amino acids 1-452 (Rattus norvegicus)

Resistance to inhibitors of cholinesterase 8 homolog A experimental SAS data
Resistance to inhibitors of cholinesterase 8 homolog A Kratky plot
Sample: Resistance to inhibitors of cholinesterase 8 homolog A monomer, 51 kDa Rattus norvegicus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2018 Apr 24
Structure, Function, and Dynamics of the Gα Binding Domain of Ric-8A. Structure (2019)
Zeng B, Mou TC, Doukov TI, Steiner A, Yu W, Papasergi-Scott M, Tall GG, Hagn F, Sprang SR
RgGuinier 3.0 nm
Dmax 10.6 nm
VolumePorod 70 nm3

SASDFB5 – Phosphorylated Resistance to inhibitors of cholinesterase 8 homolog A, Ric-8A, amino acids 1-452 (Rattus norvegicus)

Resistance to inhibitors of cholinesterase 8 homolog A experimental SAS data
Resistance to inhibitors of cholinesterase 8 homolog A Kratky plot
Sample: Resistance to inhibitors of cholinesterase 8 homolog A monomer, 51 kDa Rattus norvegicus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2018 Apr 24
Structure, Function, and Dynamics of the Gα Binding Domain of Ric-8A. Structure (2019)
Zeng B, Mou TC, Doukov TI, Steiner A, Yu W, Papasergi-Scott M, Tall GG, Hagn F, Sprang SR
RgGuinier 3.0 nm
Dmax 10.1 nm
VolumePorod 70 nm3

SASDF62 – Mixture of the dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE, and the roX2 RNA stem-loop 7 18mer-fragment, at 1.0 mg/ml

Dosage compensation regulatorroX2 stem-loop 7, 18-mer fragment experimental SAS data
Dosage compensation regulator roX2 stem-loop 7, 18-mer fragment Kratky plot
Sample: Dosage compensation regulator monomer, 29 kDa Drosophila melanogaster protein
RoX2 stem-loop 7, 18-mer fragment monomer, 12 kDa synthetic construct RNA
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 3.1 nm
Dmax 13.3 nm
VolumePorod 25 nm3

SASDDD7 – Apolipoprotein E2

Apolipoprotein E2 experimental SAS data
Apolipoprotein E2 Kratky plot
Sample: Apolipoprotein E2 tetramer, 139 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 300 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Nov 29
The molecular basis for Apolipoprotein E4 as the major risk factor for late onset Alzheimer's disease. J Mol Biol (2019)
Raulin AC, Kraft L, Al-Hilaly YK, Xue WF, McGeehan JE, Atack JR, Serpell L
RgGuinier 5.6 nm
Dmax 19.5 nm
VolumePorod 400 nm3