Browse by ORGANISM: Homo sapiens (Human)

SASDFD2 – wild-type human Latent Transforming Growth Factor beta 1 (LTGFB-1)

Human Latent Transforming Growth Factor beta 1 experimental SAS data
Human Latent Transforming Growth Factor beta 1 Kratky plot
Sample: Human Latent Transforming Growth Factor beta 1 dimer, 86 kDa Homo sapiens protein
Buffer: phosphate buffered saline 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Oct 4
Structural consequences of transforming growth factor beta-1 activation from near-therapeutic X-ray doses. J Synchrotron Radiat 26(Pt 4):967-979 (2019)
Stachowski T, Grant TD, Snell EH
RgGuinier 3.8 nm
Dmax 17.5 nm
VolumePorod 200 nm3

SASDFE2 – wild-type human Latency Associated Peptide (LAP)

Latency Associated Peptide experimental SAS data
Latency Associated Peptide Kratky plot
Sample: Latency Associated Peptide dimer, 58 kDa Homo sapiens protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Oct 4
Structural consequences of transforming growth factor beta-1 activation from near-therapeutic X-ray doses. J Synchrotron Radiat 26(Pt 4):967-979 (2019)
Stachowski T, Grant TD, Snell EH
RgGuinier 4.1 nm
Dmax 17.5 nm
VolumePorod 179 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

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, Saunders M, Hammad H, Savvides SN, Lambrecht BN
RgGuinier 2.1 nm
Dmax 8.2 nm
VolumePorod 46 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

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

SASDEC7 – Human TRPML2 Ion Channel Extracytosolic/Lumenal Domain at pH 7.4 without Calcium

Transient receptor potential channel mucolipin 2 experimental SAS data
CORAL model
Sample: Transient receptor potential channel mucolipin 2 tetramer, 93 kDa Homo sapiens protein
Buffer: 10 mM HEPES pH 7.4, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Oct 18
Structure of the Human TRPML2 Ion Channel Extracytosolic/Lumenal Domain. Structure (2019)
Viet KK, Wagner A, Schwickert K, Hellwig N, Brennich M, Bader N, Schirmeister T, Morgner N, Schindelin H, Hellmich UA
RgGuinier 3.4 nm
Dmax 8.9 nm
VolumePorod 134 nm3

SASDED7 – Human TRPML2 Ion Channel Extracytosolic/Lumenal Domain at pH 7.4, 2mM Calcium

Transient receptor potential channel mucolipin 2 experimental SAS data
CORAL model
Sample: Transient receptor potential channel mucolipin 2 tetramer, 93 kDa Homo sapiens protein
Buffer: 10 mM HEPES pH 7.4, 150 mM NaCl, 2 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Oct 20
Structure of the Human TRPML2 Ion Channel Extracytosolic/Lumenal Domain. Structure (2019)
Viet KK, Wagner A, Schwickert K, Hellwig N, Brennich M, Bader N, Schirmeister T, Morgner N, Schindelin H, Hellmich UA
RgGuinier 3.4 nm
Dmax 8.9 nm
VolumePorod 134 nm3