SASDUL2 – mRNA capping enzyme small subunit

Virus termination factor small subunit experimental SAS data
DAMFILT model
Sample: Virus termination factor small subunit monomer, 33 kDa Monkeypox virus (strain … protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2024 Jan 4
Structural basis of the monkeypox virus mRNA cap N7 methyltransferase complex. Emerg Microbes Infect 13(1):2369193 (2024)
Chen A, Fang N, Zhang Z, Wen Y, Shen Y, Zhang Y, Zhang L, Zhao G, Ding J, Li J
RgGuinier 2.4 nm
Dmax 6.8 nm
VolumePorod 51 nm3

SASDUM2 – mRNA capping enzyme MTase

Virus termination factor small subunitmRNA-capping enzyme catalytic subunit experimental SAS data
DAMFILT model
Sample: Virus termination factor small subunit monomer, 33 kDa Monkeypox virus (strain … protein
mRNA-capping enzyme catalytic subunit monomer, 35 kDa Monkeypox virus (strain … protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2024 Jan 4
Structural basis of the monkeypox virus mRNA cap N7 methyltransferase complex. Emerg Microbes Infect 13(1):2369193 (2024)
Chen A, Fang N, Zhang Z, Wen Y, Shen Y, Zhang Y, Zhang L, Zhao G, Ding J, Li J
RgGuinier 2.9 nm
Dmax 10.1 nm
VolumePorod 106 nm3

SASDU78 – Trypanosoma brucei ESAG4 membrane-proximal Venus Fly Trap domain 2 (VFT2)

adenylate cyclase experimental SAS data
ALPHAFOLD model
Sample: adenylate cyclase monomer, 43 kDa Trypanosoma brucei protein
Buffer: 50 mM Tris-HCl, 500 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2023 Sep 23
Biophysical analysis of the membrane-proximal Venus Flytrap domain of ESAG4 receptor-like adenylate cyclase from Trypanosoma brucei. Mol Biochem Parasitol 260:111653 (2024)
Alves DO, Geens R, da Silva Arruda HR, Jennen L, Corthaut S, Wuyts E, de Andrade GC, Prosdocimi F, Cordeiro Y, Pires JR, Vieira LR, de Oliveira GAP, Sterckx YG, Salmon D
RgGuinier 2.3 nm
Dmax 7.6 nm
VolumePorod 76 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

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

4733 hits found.