SASBDB entries for UniProt ID:

SASDV77 – Human Splicing Factor Proline/Glutamine rich SFPQ1 dimer with C-terminal truncation (delta599-707) in low salt buffer

UniProt ID: P23246 (1-598) Splicing Factor Proline/Glutamine rich (1-598)
Splicing Factor Proline/Glutamine rich (1-598) experimental SAS data
Splicing Factor Proline/Glutamine rich (1-598) Kratky plot
Sample: Splicing Factor Proline/Glutamine rich (1-598) dimer, 130 kDa Homo sapiens protein
Buffer: 150 mM KCl, 20 mM HEPES, 5% glycerol, 5 mM MgCl2, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2023 Mar 13
Structural dynamics of IDR interactions in human SFPQ and implications for liquid–liquid phase separation Acta Crystallographica Section D Structural Biology 81(7):357-379 (2025)
Koning H, Lai V, Sethi A, Chakraborty S, Ang C, Fox A, Duff A, Whitten A, Marshall A, Bond C
RgGuinier 6.1 nm
Dmax 28.0 nm
VolumePorod 315 nm3

SASDVC7 – Tetrameric L-threonine dehydratase biosynthetic IlvA (EcIlvA) from Eschericia coli

UniProt ID: P04968 (2-514) L-threonine dehydratase biosynthetic IlvA
L-threonine dehydratase biosynthetic IlvA experimental SAS data
CHIMERA model
Sample: L-threonine dehydratase biosynthetic IlvA tetramer, 233 kDa Escherichia coli (strain … protein
Buffer: 20 mM KPO4, 200 mM NaCl, 0.1 mM TCEP,, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Oct 14
Isoleucine Binding and Regulation of Escherichia coli and Staphylococcus aureus Threonine Dehydratase (IlvA). Biochemistry (2025)
Yun MK, Subramanian C, Miller K, Jackson P, Radka CD, Rock CO
RgGuinier 4.5 nm
Dmax 15.6 nm
VolumePorod 284 nm3

SASDVD7 – Regulatory domain of L-threonine dehydratase biosynthetic IlvA (EcIlvA) from Eschericia coli

UniProt ID: P04968 (335-514) L-threonine dehydratase biosynthetic IlvA Regulatory domain
L-threonine dehydratase biosynthetic IlvA Regulatory domain experimental SAS data
CHIMERA model
Sample: L-threonine dehydratase biosynthetic IlvA Regulatory domain dimer, 46 kDa Escherichia coli (strain … protein
Buffer: 20 mM KPO4, 200 mM NaCl, 0.1 mM TCEP,, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Oct 14
Isoleucine Binding and Regulation of Escherichia coli and Staphylococcus aureus Threonine Dehydratase (IlvA). Biochemistry (2025)
Yun MK, Subramanian C, Miller K, Jackson P, Radka CD, Rock CO
RgGuinier 2.3 nm
Dmax 8.0 nm
VolumePorod 50 nm3

SASDVE7 – Hexameric L-threonine dehydratase biosynthetic (IlvA) from Staphylococcus aureus

UniProt ID: Q2FF63 (336-422) L-threonine dehydratase biosynthetic IlvA
L-threonine dehydratase biosynthetic IlvA experimental SAS data
CHIMERA model
Sample: L-threonine dehydratase biosynthetic IlvA hexamer, 288 kDa Staphylococcus aureus (strain … protein
Buffer: 20 mM KPO4, 200 mM NaCl, 0.1 mM TCEP,, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Oct 14
Isoleucine Binding and Regulation of Escherichia coli and Staphylococcus aureus Threonine Dehydratase (IlvA). Biochemistry (2025)
Yun MK, Subramanian C, Miller K, Jackson P, Radka CD, Rock CO
RgGuinier 5.1 nm
Dmax 17.1 nm
VolumePorod 386 nm3

SASDVF7 – Third double-stranded RNA-binding domain of Human Double-stranded RNA-specific adenosine deaminase (ADAR1) (residues 688-817, i.e. dsRBD3-long)

UniProt ID: P55265 (688-817) Third double-stranded RNA-binding domain of human ADAR1 (residues 688-817, i.e. dsRBD3-long)
Third double-stranded RNA-binding domain of human ADAR1 (residues 688-817, i.e. dsRBD3-long) experimental SAS data
Third double-stranded RNA-binding domain of human ADAR1 (residues 688-817, i.e. dsRBD3-long) Kratky plot
Sample: Third double-stranded RNA-binding domain of human ADAR1 (residues 688-817, i.e. dsRBD3-long) dimer, 29 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 2.6 nm
Dmax 8.0 nm
VolumePorod 50 nm3

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

UniProt ID: P55265 (708-801) Third double-stranded RNA-binding domain of human 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)

UniProt ID: P55265 (716-797) Third double-stranded RNA-binding domain of human 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)

UniProt ID: P55265 (708-801) Third double-stranded RNA-binding domain of human 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)

UniProt ID: P55265 (708-801) Third double-stranded RNA-binding domain of human 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)

UniProt ID: P55265 (708-801) 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