Browse by ORGANISM: Homo sapiens (Human)

SASDBT3 – RNF8 (L451D mutant) complexed with Ubc13 (C87K, K92A mutant): conjugated to Ubiquitin

Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A)Polyubiquitin-CE3 ubiquitin-protein ligase RNF8 mutant (L451D) experimental SAS data
MES-FOXS model
Sample: Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A) dimer, 36 kDa Homo sapiens protein
Polyubiquitin-C dimer, 17 kDa Homo sapiens protein
E3 ubiquitin-protein ligase RNF8 mutant (L451D) dimer, 35 kDa Homo sapiens protein
Buffer: 20 mM HEPES 200 mM NaCl 0.01 mM ZnSO4 1 mM DTT, pH: 6.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Sep 8
RNF8 E3 Ubiquitin Ligase Stimulates Ubc13 E2 Conjugating Activity That Is Essential for DNA Double Strand Break Signaling and BRCA1 Tumor Suppressor Recruitment. J Biol Chem 291(18):9396-410 (2016)
Hodge CD, Ismail IH, Edwards RA, Hura GL, Xiao AT, Tainer JA, Hendzel MJ, Glover JN
RgGuinier 4.3 nm
Dmax 18.9 nm
VolumePorod 111 nm3

SASDBU3 – RNF8 (L451D mutant) complexed with Ubc13 (C87K, K92A mutant) and Mms2: conjugated to Ubiquitin

Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A)Polyubiquitin-CUbiquitin-conjugating enzyme E2 variant 2E3 ubiquitin-protein ligase RNF8 mutant (L451D) experimental SAS data
MES-FOXS model
Sample: Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A) dimer, 36 kDa Homo sapiens protein
Polyubiquitin-C dimer, 17 kDa Homo sapiens protein
Ubiquitin-conjugating enzyme E2 variant 2 dimer, 34 kDa Homo sapiens protein
E3 ubiquitin-protein ligase RNF8 mutant (L451D) dimer, 35 kDa Homo sapiens protein
Buffer: 20 mM HEPES 200 mM NaCl 0.01 mM ZnSO4 1 mM DTT, pH: 6.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Sep 8
RNF8 E3 Ubiquitin Ligase Stimulates Ubc13 E2 Conjugating Activity That Is Essential for DNA Double Strand Break Signaling and BRCA1 Tumor Suppressor Recruitment. J Biol Chem 291(18):9396-410 (2016)
Hodge CD, Ismail IH, Edwards RA, Hura GL, Xiao AT, Tainer JA, Hendzel MJ, Glover JN
RgGuinier 5.2 nm
Dmax 23.8 nm
VolumePorod 192 nm3

SASDBN2 – Human linear diubiquitin

Linear di-ubiquitin experimental SAS data
Human linear diubiquitin Rg histogram
Sample: Linear di-ubiquitin monomer, 17 kDa Homo sapiens protein
Buffer: 50 mM Tris 150 mM NaCl 1 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at 5C, Pohang Accelerator Laboratory on 2014 Nov 3
New conformations of linear polyubiquitin chains from crystallographic and solution-scattering studies expand the conformational space of polyubiquitin. Acta Crystallogr D Struct Biol 72(Pt 4):524-35 (2016)
Thach TT, Shin D, Han S, Lee S
RgGuinier 2.1 nm
Dmax 6.6 nm
VolumePorod 20 nm3

SASDBP2 – Human linear triubiquitin

Human linear tri-ubiquitin experimental SAS data
Human linear triubiquitin Rg histogram
Sample: Human linear tri-ubiquitin monomer, 26 kDa Homo sapiens protein
Buffer: 50 mM Tris 150mM NaCl 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 5C, Pohang Accelerator Laboratory on 2014 Nov 3
New conformations of linear polyubiquitin chains from crystallographic and solution-scattering studies expand the conformational space of polyubiquitin. Acta Crystallogr D Struct Biol 72(Pt 4):524-35 (2016)
Thach TT, Shin D, Han S, Lee S
RgGuinier 2.5 nm
Dmax 8.6 nm
VolumePorod 36 nm3

SASDBQ2 – Human linear tetraubiquitin

Human linear tetra-ubiquitin experimental SAS data
Human linear tetraubiquitin Rg histogram
Sample: Human linear tetra-ubiquitin monomer, 34 kDa Homo sapiens protein
Buffer: 50 mM Tris 150mM NaCl 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 5C, Pohang Accelerator Laboratory on 2014 Nov 3
New conformations of linear polyubiquitin chains from crystallographic and solution-scattering studies expand the conformational space of polyubiquitin. Acta Crystallogr D Struct Biol 72(Pt 4):524-35 (2016)
Thach TT, Shin D, Han S, Lee S
RgGuinier 3.1 nm
Dmax 11.2 nm
VolumePorod 49 nm3

SASDMU4 – Retinoic acid receptor RXR-alpha ligand binding domain (LBD)

Retinoic acid receptor RXR-alpha experimental SAS data
CUSTOM IN-HOUSE model
Sample: Retinoic acid receptor RXR-alpha dimer, 51 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl, 100 mM KCl, 5% glycerol, 2 mM Chaps, and 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Oct 7
Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein Biochemistry 55(12):1741-1748 (2016)
Belorusova A, Osz J, Petoukhov M, Peluso-Iltis C, Kieffer B, Svergun D, Rochel N
RgGuinier 2.5 nm
Dmax 8.3 nm
VolumePorod 60 nm3

SASDMV4 – Full-length Retinoic acid receptor RXR-alpha in complex with Ramp2 DNA

Retinoic acid receptor RXR-alphaRamp2 DNA experimental SAS data
EOM/RANCH model
Sample: Retinoic acid receptor RXR-alpha dimer, 102 kDa Homo sapiens protein
Ramp2 DNA monomer, 11 kDa DNA
Buffer: 20 mM Tris, 50 mM NaCl, 50 mM KCl, 5% glycerol, 2 mM Chaps, and 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 May 7
Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein Biochemistry 55(12):1741-1748 (2016)
Belorusova A, Osz J, Petoukhov M, Peluso-Iltis C, Kieffer B, Svergun D, Rochel N
RgGuinier 4.4 nm
Dmax 13.9 nm
VolumePorod 161 nm3

SASDMW4 – Retinoic acid receptor RXR-alpha N-terminal and DNA binding domains (DBD) in complex with Ramp2 DNA

Ramp2 DNARetinoic acid receptor RXR-alpha experimental SAS data
EOM/RANCH model
Sample: Ramp2 DNA monomer, 11 kDa DNA
Retinoic acid receptor RXR-alpha dimer, 44 kDa Homo sapiens protein
Buffer: 20 mM Tris, 50 mM NaCl, 50 mM KCl, 5% glycerol, 2 mM Chaps, and 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Jul 17
Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein Biochemistry 55(12):1741-1748 (2016)
Belorusova A, Osz J, Petoukhov M, Peluso-Iltis C, Kieffer B, Svergun D, Rochel N
RgGuinier 4.3 nm
Dmax 14.3 nm
VolumePorod 89 nm3

SASDMX4 – Retinoic acid receptor RXR-alpha DNA binding (DBD) and ligand binding (LBD) domains in complex with Ramp2 DNA

Ramp2 DNARetinoic acid receptor RXR-alpha experimental SAS data
CORAL model
Sample: Ramp2 DNA monomer, 11 kDa DNA
Retinoic acid receptor RXR-alpha dimer, 74 kDa Homo sapiens protein
Buffer: 20 mM Tris, 50 mM NaCl, 50 mM KCl, 5% glycerol, 2 mM Chaps, and 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Oct 7
Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein Biochemistry 55(12):1741-1748 (2016)
Belorusova A, Osz J, Petoukhov M, Peluso-Iltis C, Kieffer B, Svergun D, Rochel N
RgGuinier 3.6 nm
Dmax 12.2 nm

SASDMY4 – Retinoic acid receptor RXR-alpha DNA binding domain (DBD) in complex with Ramp2

Ramp2 DNARetinoic acid receptor RXR-alpha experimental SAS data
CUSTOM IN-HOUSE model
Sample: Ramp2 DNA monomer, 11 kDa DNA
Retinoic acid receptor RXR-alpha dimer, 20 kDa Homo sapiens protein
Buffer: 20 mM Tris, 50 mM NaCl, 50 mM KCl, 5% glycerol, 2 mM Chaps, and 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Oct 7
Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein Biochemistry 55(12):1741-1748 (2016)
Belorusova A, Osz J, Petoukhov M, Peluso-Iltis C, Kieffer B, Svergun D, Rochel N
RgGuinier 1.9 nm
Dmax 5.8 nm