SASDVU5 – Marchantia polymorpha Auxin Response Factor 3 in complex with high affinity DNA

Auxin response factorHigh Affinity ARF binding sequence inverted repeat with 6 nucleotide spacing experimental SAS data
SWISSMODEL model
Sample: Auxin response factor monomer, 46 kDa Marchantia polymorpha protein
High Affinity ARF binding sequence inverted repeat with 6 nucleotide spacing dimer, 12 kDa DNA
Buffer: 20 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BL11 - NCD, ALBA on 2019 Dec 3
The structure and function of the DNA binding domain of class B MpARF2 share more traits with class A AtARF5 than to that of class B AtARF1
Isidro Crespo
RgGuinier 3.1 nm
Dmax 8.4 nm
VolumePorod 67 nm3

SASDVV5 – Arabidopsis thaliana Auxin Response Factor 1 in complex with high affinity DNA

Auxin response factor 1High Affinity ARF binding sequence inverted repeat with 7 nucleotide spacing experimental SAS data
Auxin response factor 1 High Affinity ARF binding sequence inverted repeat with 7 nucleotide spacing Kratky plot
Sample: Auxin response factor 1 dimer, 81 kDa Arabidopsis thaliana protein
High Affinity ARF binding sequence inverted repeat with 7 nucleotide spacing dimer, 13 kDa DNA
Buffer: 20 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BL11 - NCD, ALBA on 2019 Dec 3
The structure and function of the DNA binding domain of class B MpARF2 share more traits with class A AtARF5 than to that of class B AtARF1
RgGuinier 3.6 nm
Dmax 10.5 nm
VolumePorod 136 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

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

SASDTU8 – Complement C3* at 1.25 mg/mL (pH 6.0, 200 mM NaCl)

Complement C3 (Δ668-671) experimental SAS data
CORAL model
Sample: Complement C3 (Δ668-671) monomer, 187 kDa Homo sapiens protein
Buffer: 20 mM MES pH 6.0, 200 mM NaCl, pH: 6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2022 Nov 7
Cryo-EM analysis of complement C3 reveals a reversible major opening of the macroglobulin ring
Martin Høgholm Jørgensen
RgGuinier 5.4 nm
Dmax 21.8 nm
VolumePorod 357 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

4417 hits found.