Browse by ORGANISM: Homo sapiens (Human)

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

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

SASDNX3 – Calcium-bound Calmodulin, including structural models

Calmodulin-1 experimental SAS data
Calcium-bound Calmodulin, including structural models Rg histogram
Sample: Calmodulin-1 monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM Hepes, 150 mM NaCl, 2 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Nov 15
Dynamics and structural changes of calmodulin upon interaction with the antagonist calmidazolium. BMC Biol 20(1):176 (2022)
Léger C, Pitard I, Sadi M, Carvalho N, Brier S, Mechaly A, Raoux-Barbot D, Davi M, Hoos S, Weber P, Vachette P, Durand D, Haouz A, Guijarro JI, Ladant D, Chenal A
RgGuinier 2.2 nm
Dmax 7.2 nm
VolumePorod 33 nm3

SASDNY3 – Calcium-bound Calmodulin complexed with Calmidazolium

Calmodulin-1Calmidazolium experimental SAS data
Sample: Calmodulin-1 monomer, 17 kDa Homo sapiens protein
Calmidazolium monomer, 1 kDa
Buffer: 20 mM Hepes, 150 mM NaCl, 2 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Nov 15
Dynamics and structural changes of calmodulin upon interaction with the antagonist calmidazolium. BMC Biol 20(1):176 (2022)
Léger C, Pitard I, Sadi M, Carvalho N, Brier S, Mechaly A, Raoux-Barbot D, Davi M, Hoos S, Weber P, Vachette P, Durand D, Haouz A, Guijarro JI, Ladant D, Chenal A
RgGuinier 1.7 nm
Dmax 5.2 nm
VolumePorod 30 nm3

SASDN97 – Human thryoglobulin measured using SEC-SAXS

Thyroglobulin experimental SAS data
DAMMIN model
Sample: Thyroglobulin dimer, 610 kDa Homo sapiens protein
Buffer: phosphate buffered saline, 150mM NaCl, pH: 8
Experiment: SAXS data collected at 16-ID (LiX), National Synchrotron Light Source II (NSLS-II) on 2020 Jul 17
Thyroglobulin - human and bovine SAXS/WAXS data
James Byrnes
RgGuinier 7.7 nm
Dmax 26.3 nm
VolumePorod 1800 nm3

SASDJJ5 – Histone H2A:H2B:H3:H4 complex with aprataxin and polynucleotide kinase like factor (APLF) acidic domain

Aprataxin and PNK-like factor (acidic domain)Histone H2AHistone H2BHistone H3Histone H4 experimental SAS data
DAMMIF model
Sample: Aprataxin and PNK-like factor (acidic domain) dimer, 15 kDa Homo sapiens protein
Histone H2A dimer, 26 kDa Drosophila melanogaster protein
Histone H2B dimer, 27 kDa Drosophila melanogaster protein
Histone H3 dimer, 30 kDa Drosophila melanogaster protein
Histone H4 dimer, 23 kDa Drosophila melanogaster protein
Buffer: 25 mM NaPi, 300 mM NaCl, 3% v/v glycerol, 1 mM DTT,, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 10
Chaperoning of the histone octamer by the acidic domain of DNA repair factor APLF. Sci Adv 8(30):eabo0517 (2022)
Corbeski I, Guo X, Eckhardt BV, Fasci D, Wiegant W, Graewert MA, Vreeken K, Wienk H, Svergun DI, Heck AJR, van Attikum H, Boelens R, Sixma TK, Mattiroli F, van Ingen H
RgGuinier 3.7 nm
Dmax 10.8 nm
VolumePorod 260 nm3