Browse by MODEL: Hybrid

SASDKA6 – Flavonoid-responsive regulator A (FrrA)

TetR/AcrR family transcriptional regulator experimental SAS data
CORAL model
Sample: TetR/AcrR family transcriptional regulator dimer, 48 kDa Bradyrhizobium diazoefficiens protein
Buffer: 20 mM Na2HPO4, 50 mM NaCl, 50 mM imidazole, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Sep 23
The Induction Mechanism of the Flavonoid-Responsive Regulator FrrA. FEBS J (2021)
Werner N, Werten S, Hoppen J, Palm GJ, Göttfert M, Hinrichs W
RgGuinier 3.4 nm
Dmax 9.0 nm
VolumePorod 93 nm3

SASDL82 – Human acetylcholinesterase, apo

acetylcholinesteraseacetylcholinesterase experimental SAS data
OTHER model
Sample: Acetylcholinesterase dimer, 120 kDa Homo sapiens protein
Acetylcholinesterase monomer, 60 kDa Homo sapiens protein
Buffer: 50 mM Tris/HCl, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 May 29
Covalent inhibition of hAChE by organophosphates causes homodimer dissociation through long-range allosteric effects. J Biol Chem :101007 (2021)
Blumenthal DK, Cheng X, Fajer M, Ho KY, Rohrer J, Gerlits O, Taylor P, Juneja P, Kovalevsky A, Radić Z
RgGuinier 3.9 nm
Dmax 13.0 nm
VolumePorod 162 nm3

SASDL92 – Human acetylcholinesterase, covalently bound to paraoxon

acetylcholinesteraseacetylcholinesterase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Acetylcholinesterase dimer, 120 kDa Homo sapiens protein
Acetylcholinesterase monomer, 60 kDa Homo sapiens protein
Buffer: 50 mM Tris/HCl, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 May 29
Covalent inhibition of hAChE by organophosphates causes homodimer dissociation through long-range allosteric effects. J Biol Chem :101007 (2021)
Blumenthal DK, Cheng X, Fajer M, Ho KY, Rohrer J, Gerlits O, Taylor P, Juneja P, Kovalevsky A, Radić Z
RgGuinier 3.4 nm
Dmax 12.0 nm
VolumePorod 142 nm3

SASDLZ2 – Immunoglobulin G3 (IgG3) Glycosylated

Immunoglobulin G subclass 3 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Immunoglobulin G subclass 3 monomer, 155 kDa Homo sapiens protein
Buffer: 20 mM L-histidine, 138 mM NaCl, and 2.6 mM KCl buffer, pH: 6
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Jul 29
Solution structures of human myeloma IgG3 antibody reveal extended Fab and Fc regions relative to the other IgG subclasses. J Biol Chem :100995 (2021)
Spiteri VA, Goodall M, Doutch J, Rambo RP, Gor J, Perkins SJ
RgGuinier 7.0 nm
Dmax 22.9 nm
VolumePorod 267 nm3

SASDL23 – Immunoglobulin G3 (IgG3) Deglycosylated

Immunoglobulin G subclass 3 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Immunoglobulin G subclass 3 monomer, 155 kDa Homo sapiens protein
Buffer: 20 mM L-histidine, 138 mM NaCl, and 2.6 mM KCl buffer, pH: 6
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Jul 29
Solution structures of human myeloma IgG3 antibody reveal extended Fab and Fc regions relative to the other IgG subclasses. J Biol Chem :100995 (2021)
Spiteri VA, Goodall M, Doutch J, Rambo RP, Gor J, Perkins SJ
RgGuinier 7.1 nm
Dmax 27.7 nm
VolumePorod 294 nm3

SASDL46 – 14-3-3zeta AXH-C complex

14-3-3 protein zeta/deltaAtaxin-1 AXH-C experimental SAS data
MULTIFOXS model
Sample: 14-3-3 protein zeta/delta dimer, 53 kDa Homo sapiens protein
Ataxin-1 AXH-C dimer, 55 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Oct 13
A structural study of the cytoplasmic chaperone effect of 14-3-3 proteins on Ataxin-1. J Mol Biol :167174 (2021)
Leysen S, Jane Burnley R, Rodriguez E, Milroy LG, Soini L, Adamski CJ, Nitschke L, Davis R, Obsil T, Brunsveld L, Crabbe T, Yahya Zoghbi H, Ottmann C, Martin Davis J
RgGuinier 4.8 nm
Dmax 19.8 nm

SASDK36 – LC-18t - ssDNA aptamer specific to lung adenocarcinoma cancer cells

Lung adenocarcinoma aptamer, truncated version experimental SAS data
GROMACS model
Sample: Lung adenocarcinoma aptamer, truncated version monomer, 11 kDa Artificially synthesized DNA
Buffer: Phosphate-buffered saline, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Oct 28
The Role of Small-Angle X-Ray Scattering and Molecular Simulations in 3D Structure Elucidation of a DNA Aptamer Against Lung Cancer Molecular Therapy - Nucleic Acids (2021)
Morozov D, Mironov V, Moryachkov R, Shchugoreva I, Artyushenko P, Zamay G, Kolovskaya O, Zamay T, Krat A, Molodenskiy D, Zabluda V, Veprintsev D, Sokolov A, Zukov R, Berezovski M, Tomilin F, Fedorov D, Alexeev Y, Kichkailo A
RgGuinier 2.1 nm
Dmax 6.7 nm
VolumePorod 16 nm3

SASDJN2 – Tyrosyl-DNA phosphodiesterase 1 (TDP1)

Tyrosyl-DNA phosphodiesterase 1 experimental SAS data
BILBOMD model
Sample: Tyrosyl-DNA phosphodiesterase 1 monomer, 71 kDa Homo sapiens protein
Buffer: 200 mM NaCl, 20 mM Tris-HCl, pH 7.5, 2% glycerol,, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 26
Direct interaction of DNA repair protein tyrosyl DNA phosphodiesterase 1 and the DNA ligase III catalytic domain is regulated by phosphorylation of its flexible N-terminus. J Biol Chem :100921 (2021)
Rashid I, Hammel M, Sverzhinsky A, Tsai MS, Pascal JM, Tainer JA, Tomkinson AE
RgGuinier 3.2 nm
Dmax 11.7 nm
VolumePorod 143 nm3

SASDJP2 – Truncated tyrosyl-DNA phosphodiesterase 1 (TDP1 149-608)

Tyrosyl-DNA phosphodiesterase 1 (149-608) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Tyrosyl-DNA phosphodiesterase 1 (149-608) monomer, 53 kDa Homo sapiens protein
Buffer: 200 mM NaCl, 20 mM Tris-HCl, pH 7.5, 2% glycerol,, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Sep 18
Direct interaction of DNA repair protein tyrosyl DNA phosphodiesterase 1 and the DNA ligase III catalytic domain is regulated by phosphorylation of its flexible N-terminus. J Biol Chem :100921 (2021)
Rashid I, Hammel M, Sverzhinsky A, Tsai MS, Pascal JM, Tainer JA, Tomkinson AE
RgGuinier 2.3 nm
Dmax 7.0 nm
VolumePorod 80 nm3

SASDJQ2 – Dephosphorylated tyrosyl-DNA phosphodiesterase 1 (TDP1-Ppi)

Tyrosyl-DNA phosphodiesterase 1 (dephosphorylated) experimental SAS data
BILBOMD model
Sample: Tyrosyl-DNA phosphodiesterase 1 (dephosphorylated) monomer, 71 kDa Homo sapiens protein
Buffer: 200 mM NaCl, 20 mM Tris-HCl, pH 7.5, 2% glycerol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 26
Direct interaction of DNA repair protein tyrosyl DNA phosphodiesterase 1 and the DNA ligase III catalytic domain is regulated by phosphorylation of its flexible N-terminus. J Biol Chem :100921 (2021)
Rashid I, Hammel M, Sverzhinsky A, Tsai MS, Pascal JM, Tainer JA, Tomkinson AE
RgGuinier 3.2 nm
Dmax 16.5 nm
VolumePorod 141 nm3