Browse by ORGANISM: Homo sapiens (Human)

SASDUQ9 – Wild-type Importin Beta Binding domain (IBB) from importin subunit alpha-1 in 2 M Urea

Importin subunit alpha-1 experimental SAS data
Importin subunit alpha-1 Kratky plot
Sample: Importin subunit alpha-1 monomer, 9 kDa Homo sapiens protein
Buffer: phosphate buffered saline containing 2 M urea, 0.3 M KCl, 5 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Jul 1
A genetically encoded anomalous SAXS ruler to probe the dimensions of intrinsically disordered proteins. Proc Natl Acad Sci U S A 121(50):e2415220121 (2024)
Yu M, Gruzinov AY, Ruan H, Scheidt T, Chowdhury A, Giofrè S, Mohammed ASA, Caria J, Sauter PF, Svergun DI, Lemke EA
RgGuinier 2.7 nm
Dmax 11.8 nm
VolumePorod 22 nm3

SASDUR9 – Br-labelled Importin Beta Binding domain (IBB) from importin subunit alpha-1 in 6 M Urea

importin-beta-binding domain of importin subunit alpha-1 labelled with unnatural amino acid diBrK experimental SAS data
importin-beta-binding domain of importin subunit alpha-1 labelled with unnatural amino acid diBrK Kratky plot
Sample: Importin-beta-binding domain of importin subunit alpha-1 labelled with unnatural amino acid diBrK monomer, 8 kDa Homo sapiens protein
Buffer: phosphate buffered saline containing 6 M urea, 0.3 M KCl, 5 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Dec 19
A genetically encoded anomalous SAXS ruler to probe the dimensions of intrinsically disordered proteins. Proc Natl Acad Sci U S A 121(50):e2415220121 (2024)
Yu M, Gruzinov AY, Ruan H, Scheidt T, Chowdhury A, Giofrè S, Mohammed ASA, Caria J, Sauter PF, Svergun DI, Lemke EA
RgGuinier 3.0 nm
Dmax 12.3 nm
VolumePorod 28 nm3

SASDVQ6 – Retriever complex

VPS35 endosomal protein-sorting factor-likeVacuolar protein sorting-associated protein 29Vacuolar protein sorting-associated protein 26C experimental SAS data
ALPHAFOLD model
Sample: VPS35 endosomal protein-sorting factor-like monomer, 110 kDa Homo sapiens protein
Vacuolar protein sorting-associated protein 29 monomer, 21 kDa Homo sapiens protein
Vacuolar protein sorting-associated protein 26C monomer, 33 kDa Homo sapiens protein
Buffer: 50 mM Tris, 200 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Apr 28
Selective cargo and membrane recognition by SNX17 regulates its interaction with Retriever EMBO Reports (2024)
Martín-González A, Méndez-Guzmán I, Zabala-Zearreta M, Quintanilla A, García-López A, Martínez-Lombardía E, Albesa-Jové D, Acosta J, Lucas M
RgGuinier 5.2 nm
Dmax 21.5 nm
VolumePorod 256 nm3

SASDVR6 – Vacuolar protein sorting-associated protein 26C (VPS26C)

Vacuolar protein sorting-associated protein 26C experimental SAS data
ALPHAFOLD model
Sample: Vacuolar protein sorting-associated protein 26C monomer, 33 kDa Homo sapiens protein
Buffer: 50 mM Tris, 150 mM NaCl, 1 mM TCEP,, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2021 Apr 22
Selective cargo and membrane recognition by SNX17 regulates its interaction with Retriever EMBO Reports (2024)
Martín-González A, Méndez-Guzmán I, Zabala-Zearreta M, Quintanilla A, García-López A, Martínez-Lombardía E, Albesa-Jové D, Acosta J, Lucas M
RgGuinier 2.7 nm
Dmax 9.4 nm
VolumePorod 44 nm3

SASDVF7 – Third double-stranded RNA-binding domain of Human Double-stranded RNA-specific adenosine deaminase (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)

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