Browse by DISSEMINATION: Published

SASDNK6 – Retinoblastoma protein at 1 mg/ml

Retinoblastoma-associated protein experimental SAS data
Retinoblastoma-associated protein Kratky plot
Sample: Retinoblastoma-associated protein monomer, 41 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 14
Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nat Struct Mol Biol (2022)
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB
RgGuinier 2.4 nm
Dmax 7.4 nm
VolumePorod 66 nm3

SASDNL6 – Retinoblastoma protein at 2 mg/ml

Retinoblastoma-associated protein experimental SAS data
Retinoblastoma-associated protein Kratky plot
Sample: Retinoblastoma-associated protein monomer, 41 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 14
Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nat Struct Mol Biol (2022)
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB
RgGuinier 2.5 nm
Dmax 7.9 nm
VolumePorod 64 nm3

SASDNM6 – Retinoblastoma protein at 4 mg/ml

Retinoblastoma-associated protein experimental SAS data
Retinoblastoma-associated protein Kratky plot
Sample: Retinoblastoma-associated protein monomer, 41 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 14
Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nat Struct Mol Biol (2022)
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB
RgGuinier 2.6 nm
Dmax 10.0 nm
VolumePorod 68 nm3

SASDNN6 – Early E1A protein at 4.2 mg/ml

Early E1A protein experimental SAS data
Early E1A protein Kratky plot
Sample: Early E1A protein monomer, 13 kDa Human adenovirus C … protein
Buffer: 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Mar 24
Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nat Struct Mol Biol (2022)
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB
RgGuinier 4.0 nm

SASDNP6 – Early E1A protein at 5.6 mg/ml

Early E1A protein experimental SAS data
Early E1A protein Kratky plot
Sample: Early E1A protein monomer, 13 kDa Human adenovirus C … protein
Buffer: 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Mar 24
Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nat Struct Mol Biol (2022)
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB
RgGuinier 4.2 nm

SASDNQ6 – Early E1A protein at 7.0 mg/ml

Early E1A protein experimental SAS data
Early E1A protein Kratky plot
Sample: Early E1A protein monomer, 13 kDa Human adenovirus C … protein
Buffer: 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Mar 24
Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nat Struct Mol Biol (2022)
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB
RgGuinier 4.1 nm

SASDNR6 – Retinoblastoma protein/Early E1A protein (RB-E1A) complex at 0.7 mg/ml

Retinoblastoma-associated proteinEarly E1A protein experimental SAS data
Retinoblastoma-associated protein Early E1A protein Kratky plot
Sample: Retinoblastoma-associated protein monomer, 41 kDa Homo sapiens protein
Early E1A protein monomer, 13 kDa Human adenovirus C … protein
Buffer: 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 14
Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nat Struct Mol Biol (2022)
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB
RgGuinier 2.9 nm
Dmax 10.0 nm
VolumePorod 80 nm3

SASDNS6 – Retinoblastoma protein/Early E1A protein (RB-E1A) complex at 1.4 mg/ml

Retinoblastoma-associated proteinEarly E1A protein experimental SAS data
Retinoblastoma-associated protein Early E1A protein Kratky plot
Sample: Retinoblastoma-associated protein monomer, 41 kDa Homo sapiens protein
Early E1A protein monomer, 13 kDa Human adenovirus C … protein
Buffer: 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 14
Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nat Struct Mol Biol (2022)
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB
RgGuinier 3.0 nm
Dmax 12.0 nm
VolumePorod 84 nm3

SASDNT6 – Retinoblastoma protein/Early E1A protein (RB-E1A) complex at 2.7 mg/ml

Retinoblastoma-associated proteinEarly E1A protein experimental SAS data
Retinoblastoma-associated protein Early E1A protein Kratky plot
Sample: Retinoblastoma-associated protein monomer, 41 kDa Homo sapiens protein
Early E1A protein monomer, 13 kDa Human adenovirus C … protein
Buffer: 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 14
Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nat Struct Mol Biol (2022)
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB
RgGuinier 3.3 nm
Dmax 17.0 nm
VolumePorod 93 nm3

SASDNU6 – Retinoblastoma protein/Early E1A protein (RB-E1A) complex - merged data from concentration series measurements

Retinoblastoma-associated proteinEarly E1A protein experimental SAS data
Retinoblastoma-associated protein Early E1A protein Kratky plot
Sample: Retinoblastoma-associated protein monomer, 41 kDa Homo sapiens protein
Early E1A protein monomer, 13 kDa Human adenovirus C … protein
Buffer: 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 14
Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nat Struct Mol Biol (2022)
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB
RgGuinier 3.0 nm
Dmax 12.0 nm
VolumePorod 84 nm3