SASDPX7 – DNA protection during starvation protein (Dps) loaded with FeSO4⋅7H2O in the amount corresponding to 50 iron atoms per dodecamer. Anomalous SAXS spanning the X-ray Fe-absorption edge 7.100-7.133 keV.

DNA protection during starvation protein experimental SAS data
DAMMIN model
Sample: DNA protection during starvation protein dodecamer, 224 kDa Escherichia coli (strain … protein
Buffer: 50 mM NaCl, 0.5 mM EDTA, 50 mM Tris-HCl, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Oct 5
Anomalous small-angle X-ray scattering study of the formation of iron clusters in the inner cavity of the ferritin-like protein Dps
RgGuinier 3.8 nm
Dmax 14.0 nm
VolumePorod 32 nm3

SASDPY7 – DNA protection during starvation protein (Dps) loaded with FeSO4⋅7H2O in the amount corresponding to 500 iron atoms per dodecamer. Anomalous SAXS spanning the X-ray Fe-absorption edge 7.100-7.133 keV.

DNA protection during starvation protein experimental SAS data
DAMMIN model
Sample: DNA protection during starvation protein dodecamer, 224 kDa Escherichia coli (strain … protein
Buffer: 50 mM NaCl, 0.5 mM EDTA, 50 mM Tris-HCl, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Oct 5
Anomalous small-angle X-ray scattering study of the formation of iron clusters in the inner cavity of the ferritin-like protein Dps
Alexander Gordienko
RgGuinier 7.4 nm
Dmax 12.0 nm

SASDPZ7 – DNA protection during starvation protein (Dps) loaded with FeSO4⋅7H2O in the amount corresponding to 2000 iron atoms per dodecamer. Anomalous SAXS spanning the X-ray Fe-absorption edge 7.100-7.133 keV...

DNA protection during starvation protein experimental SAS data
DAMMIN model
Sample: DNA protection during starvation protein dodecamer, 224 kDa Escherichia coli (strain … protein
Buffer: 50 mM NaCl, 0.5 mM EDTA, 50 mM Tris-HCl, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Oct 5
Anomalous small-angle X-ray scattering study of the formation of iron clusters in the inner cavity of the ferritin-like protein Dps
RgGuinier 7.1 nm
Dmax 14.0 nm

SASDMD9 – 7SK small nuclear RNA stem loop-1 bound to the arginine rich motif of HIV-1 Tat Group M, Subtype G

Homo sapiens RNA component of 7SK nuclear ribonucleoprotein (RN7SK), small nuclear RNAProtein Tat experimental SAS data
Homo sapiens RNA component of 7SK nuclear ribonucleoprotein (RN7SK), small nuclear RNA Protein Tat Kratky plot
Sample: Homo sapiens RNA component of 7SK nuclear ribonucleoprotein (RN7SK), small nuclear RNA monomer, 18 kDa Homo sapiens RNA
Protein Tat monomer, 2 kDa Human immunodeficiency virus … protein
Buffer: 10 mM phosphate, 70 mM NaCl, 0.1 mM EDTA, pH: 5.6
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Nov 27
A structure-based mechanism for displacement of the HEXIM adapter from 7SK small nuclear RNA. Commun Biol 5(1):819 (2022)
Pham VV, Gao M, Meagher JL, Smith JL, D'Souza VM
RgGuinier 2.5 nm
Dmax 9.9 nm
VolumePorod 28 nm3

SASDME9 – 7SK stem-loop 1 with HEXIM Arginine Rich Motif

Homo sapiens RNA component of 7SK nuclear ribonucleoprotein (RN7SK), small nuclear RNAProtein HEXIM1 experimental SAS data
Homo sapiens RNA component of 7SK nuclear ribonucleoprotein (RN7SK), small nuclear RNA Protein HEXIM1 Kratky plot
Sample: Homo sapiens RNA component of 7SK nuclear ribonucleoprotein (RN7SK), small nuclear RNA monomer, 18 kDa Homo sapiens RNA
Protein HEXIM1 monomer, 2 kDa Homo sapiens protein
Buffer: 10 mM phosphate, 70 mM NaCl, 0.1 mM EDTA, pH: 5.6
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Nov 27
A structure-based mechanism for displacement of the HEXIM adapter from 7SK small nuclear RNA. Commun Biol 5(1):819 (2022)
Pham VV, Gao M, Meagher JL, Smith JL, D'Souza VM
RgGuinier 2.2 nm
Dmax 8.2 nm
VolumePorod 26 nm3

SASDMF9 – 7SK small nuclear RNA stem loop-1 bound to the arginine rich motif of HIV-1 Tat Group M, Subtype B (Isolate A18188)

Protein TatHomo sapiens RNA component of 7SK nuclear ribonucleoprotein (RN7SK), small nuclear RNA experimental SAS data
Protein Tat Homo sapiens RNA component of 7SK nuclear ribonucleoprotein (RN7SK), small nuclear RNA Kratky plot
Sample: Protein Tat monomer, 2 kDa Human immunodeficiency virus … protein
Homo sapiens RNA component of 7SK nuclear ribonucleoprotein (RN7SK), small nuclear RNA monomer, 18 kDa Homo sapiens RNA
Buffer: 10 mM phosphate, 70 mM NaCl, 0.1 mM EDTA, pH: 5.6
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Sep 9
A structure-based mechanism for displacement of the HEXIM adapter from 7SK small nuclear RNA. Commun Biol 5(1):819 (2022)
Pham VV, Gao M, Meagher JL, Smith JL, D'Souza VM
RgGuinier 2.3 nm
Dmax 9.7 nm
VolumePorod 28 nm3

SASDPZ3 – Complex of XPA1-239 and RPAΔ32NΔ70N complex engaged on 3’ss-ds DNA junction NER substrate

DNA repair protein complementing XP-A cellsReplication protein A 70 kDa DNA-binding subunitReplication protein A 32 kDa subunitReplication protein A 14 kDa subunit3-prime ss-ds DNA junction NER model substrate experimental SAS data
MES-FOXS model
Sample: DNA repair protein complementing XP-A cells monomer, 27 kDa Homo sapiens protein
Replication protein A 70 kDa DNA-binding subunit monomer, 49 kDa Homo sapiens protein
Replication protein A 32 kDa subunit monomer, 25 kDa Homo sapiens protein
Replication protein A 14 kDa subunit monomer, 14 kDa Homo sapiens protein
3-prime ss-ds DNA junction NER model substrate monomer, 17 kDa DNA
Buffer: 20 mM Tris pH 8.0, 150 mM NaCl, 2% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Mar 4
Two interaction surfaces between XPA and RPA organize the preincision complex in nucleotide excision repair Proceedings of the National Academy of Sciences 119(34) (2022)
Kim M, Kim H, D’Souza A, Gallagher K, Jeong E, Topolska-Wós A, Ogorodnik Le Meur K, Tsai C, Tsai M, Kee M, Tainer J, Yeo J, Chazin W, Schärer O
RgGuinier 4.3 nm
Dmax 14.7 nm
VolumePorod 189 nm3

SASDP24 – Complex of XPA1-239 and RPAΔ32NΔ70N complex engaged on 5’ss-ds DNA junction NER substrate

Replication protein A 14 kDa subunitDNA repair protein complementing XP-A cellsReplication protein A 70 kDa DNA-binding subunitReplication protein A 32 kDa subunit5-prime ss-ds DNA junction NER model substrate experimental SAS data
MES-FOXS model
Sample: Replication protein A 14 kDa subunit monomer, 14 kDa Homo sapiens protein
DNA repair protein complementing XP-A cells monomer, 27 kDa Homo sapiens protein
Replication protein A 70 kDa DNA-binding subunit monomer, 49 kDa Homo sapiens protein
Replication protein A 32 kDa subunit monomer, 25 kDa Homo sapiens protein
5-prime ss-ds DNA junction NER model substrate monomer, 17 kDa DNA
Buffer: 20 mM Tris pH 8.0, 150 mM NaCl, 2% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Mar 4
Two interaction surfaces between XPA and RPA organize the preincision complex in nucleotide excision repair Proceedings of the National Academy of Sciences 119(34) (2022)
Kim M, Kim H, D’Souza A, Gallagher K, Jeong E, Topolska-Wós A, Ogorodnik Le Meur K, Tsai C, Tsai M, Kee M, Tainer J, Yeo J, Chazin W, Schärer O
RgGuinier 4.6 nm
Dmax 16.5 nm
VolumePorod 220 nm3

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, Bern...
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, Bern...
RgGuinier 2.5 nm
Dmax 7.9 nm
VolumePorod 64 nm3

2828 hits found.