Browse by MACROMOLECULE type: protein

SASDVG7 – Third double-stranded RNA-binding domain of Human Double-stranded RNA-specific adenosine deaminase (ADAR1) (residues 708-801, i.e. dsRBD3-mid)

Third double-stranded RNA-binding domain of human ADAR1 (residues 708-801, i.e. dsRBD3-mid) experimental SAS data
Third double-stranded RNA-binding domain of human ADAR1 (residues 708-801, i.e. dsRBD3-mid) Kratky plot
Sample: Third double-stranded RNA-binding domain of human ADAR1 (residues 708-801, i.e. dsRBD3-mid) dimer, 22 kDa Homo sapiens protein
Buffer: 20 mM Na-HEPES, 55 mM KOAc, 10 mM NaCl, 1 mM TCEP, pH: 7.3
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Jun 27
Dimerization of ADAR1 modulates site-specificity of RNA editing Nature Communications 15(1) (2024)
Mboukou A, Rajendra V, Messmer S, Mandl T, Catala M, Tisné C, Jantsch M, Barraud P
RgGuinier 2.0 nm
Dmax 6.7 nm
VolumePorod 27 nm3

SASDVH7 – Third double-stranded RNA-binding domain of Human Double-stranded RNA-specific adenosine deaminase (ADAR1) (residues 716-797, i.e. dsRBD3-short)

Third double-stranded RNA-binding domain of human ADAR1 (residues 716-797, i.e. dsRBD3-short) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Third double-stranded RNA-binding domain of human ADAR1 (residues 716-797, i.e. dsRBD3-short) dimer, 18 kDa Homo sapiens protein
Buffer: 20 mM Na-HEPES, 55 mM KOAc, 10 mM NaCl, 1 mM TCEP, pH: 7.3
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Jun 27
Dimerization of ADAR1 modulates site-specificity of RNA editing Nature Communications 15(1) (2024)
Mboukou A, Rajendra V, Messmer S, Mandl T, Catala M, Tisné C, Jantsch M, Barraud P
RgGuinier 1.9 nm
Dmax 5.5 nm
VolumePorod 27 nm3

SASDVJ7 – Third double-stranded RNA-binding domain of Human Double-stranded RNA-specific adenosine deaminase (ADAR1) (wild-type, residues 708-801, i.e. ADAR1-dsRBD3)

Third double-stranded RNA-binding domain of human ADAR1 (wild-type, residues 708-801, i.e. ADAR1-dsRBD3) experimental SAS data
Third double-stranded RNA-binding domain of human ADAR1 (wild-type, residues 708-801, i.e. ADAR1-dsRBD3) Kratky plot
Sample: Third double-stranded RNA-binding domain of human ADAR1 (wild-type, residues 708-801, i.e. ADAR1-dsRBD3) dimer, 25 kDa Homo sapiens protein
Buffer: 20 mM Na-phosphate, 100 mM NaCl, 2 mM 2-mercaptoethanol, pH: 7
Experiment: SAXS data collected at SWING, SOLEIL on 2021 Oct 8
Dimerization of ADAR1 modulates site-specificity of RNA editing Nature Communications 15(1) (2024)
Mboukou A, Rajendra V, Messmer S, Mandl T, Catala M, Tisné C, Jantsch M, Barraud P
RgGuinier 2.4 nm
Dmax 9.1 nm
VolumePorod 39 nm3

SASDVK7 – Third double-stranded RNA-binding domain of Human Double-stranded RNA-specific adenosine deaminase ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant)

Third double-stranded RNA-binding domain of human ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant) experimental SAS data
Third double-stranded RNA-binding domain of human ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant) Kratky plot
Sample: Third double-stranded RNA-binding domain of human ADAR1 (interface mutant, residues 708-801, i.e. ADAR1-dsRBD3 interface mutant) monomer, 12 kDa Homo sapiens protein
Buffer: 20 mM Na-phosphate, 100 mM NaCl, 2 mM 2-mercaptoethanol, pH: 7
Experiment: SAXS data collected at SWING, SOLEIL on 2021 Oct 8
Dimerization of ADAR1 modulates site-specificity of RNA editing Nature Communications 15(1) (2024)
Mboukou A, Rajendra V, Messmer S, Mandl T, Catala M, Tisné C, Jantsch M, Barraud P
RgGuinier 2.1 nm
Dmax 7.2 nm
VolumePorod 20 nm3

SASDVL7 – Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2)

Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2) experimental SAS data
Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2) Kratky plot
Sample: Chimeric construct between the third dsRBD of human ADAR1 and the second dsRBD of Xenopus Xlrbpa (chimeric construct, residues 708-801, i.e. Chimeric ADAR1-ds3/Xlrbpa-ds2) monomer, 13 kDa Homo sapiens / … protein
Buffer: 20 mM Na-phosphate, 100 mM NaCl, 2 mM 2-mercaptoethanol, pH: 7
Experiment: SAXS data collected at SWING, SOLEIL on 2021 Oct 8
Dimerization of ADAR1 modulates site-specificity of RNA editing Nature Communications 15(1) (2024)
Mboukou A, Rajendra V, Messmer S, Mandl T, Catala M, Tisné C, Jantsch M, Barraud P
RgGuinier 2.0 nm
Dmax 6.4 nm
VolumePorod 16 nm3

SASDVQ9 – Full-length mature human mitochondrial ATP synthase subunit O (Oligomycin Sensitivity Conferral Protein or Complex V subunit O)

ATP synthase subunit O, mitochondrial experimental SAS data
ALPHAFOLD model
Sample: ATP synthase subunit O, mitochondrial dimer, 42 kDa Homo sapiens protein
Buffer: 50 mM Na2HPO4, 300 mM NaCl, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2022 Mar 15
Unveiling the structural properties of the ATP Synthase subunit OSCP by SAXS
Gabriele Giachin
RgGuinier 3.7 nm
Dmax 12.0 nm
VolumePorod 78 nm3

SASDVR9 – C-terminal tail of human mitochondrial ATP synthase subunit O (137-213) (Oligomycin Sensitivity Conferral Protein or Complex V subunit O)

ATP synthase subunit O, mitochondrial C-terminal section experimental SAS data
ALPHAFOLD model
Sample: ATP synthase subunit O, mitochondrial C-terminal section trimer, 25 kDa Homo sapiens protein
Buffer: 50 mM Na2HPO4, 300 mM NaCl, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2022 Mar 15
Unveiling the structural properties of the ATP Synthase subunit OSCP by SAXS
Gabriele Giachin
RgGuinier 2.1 nm
Dmax 6.5 nm
VolumePorod 32 nm3

SASDVT9 – BioSAXS Analysis of Xylose Isomerase from Bacteroides thetaiotaomicron in PBS

Xylose isomerase experimental SAS data
DAMMIN model
Sample: Xylose isomerase tetramer, 196 kDa Bacteroides thetaiotaomicron (strain … protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at BioSAXS, Australian Synchrotron on 2024 Oct 22
BioSAXS Australian Synchrotron Standard Protein
Annmaree Warrender
RgGuinier 3.5 nm
Dmax 9.9 nm
VolumePorod 222 nm3

SASDVJ6 – apo Dipeptidyl peptidase 8 (DPP8 apo)

Isoform 1 of Dipeptidyl peptidase 8 experimental SAS data
BILBOMD model
Sample: Isoform 1 of Dipeptidyl peptidase 8 dimer, 208 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2023 Oct 14
Computational study of DPP8 and DPP9: fundamental insights and inhibitor design University of Antwerp PhD thesis c:irua:209673 (2024)
Olivier Beyens, Yann Sterckx
RgGuinier 4.2 nm
Dmax 13.6 nm
VolumePorod 271 nm3

SASDVK6 – Dipeptidyl peptidase 8 (DPP8) with compound 42

Isoform 1 of Dipeptidyl peptidase 8 experimental SAS data
BILBOMD model
Sample: Isoform 1 of Dipeptidyl peptidase 8 dimer, 208 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2023 Oct 14
Computational study of DPP8 and DPP9: fundamental insights and inhibitor design University of Antwerp PhD thesis c:irua:209673 (2024)
Olivier Beyens, Yann Sterckx
RgGuinier 4.2 nm
Dmax 13.7 nm
VolumePorod 277 nm3