Browse by ORGANISM: Homo sapiens (Human)

SASDMY6 – single-stranded DNA dC->dU-editing enzyme APOBEC3G full length

DNA dC->dU-editing enzyme APOBEC-3G experimental SAS data
DAMFILT model
Sample: DNA dC->dU-editing enzyme APOBEC-3G tetramer, 186 kDa Homo sapiens protein
Buffer: 50 mM phosphate pH 6.0, 200 mM NaCl, 2 mM β-mercaptoethanol (β-ME), 5% glycerol, 200 µM Na2-EDTA, pH: 6
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Aug 6
Small-Angle X-ray Scattering (SAXS) Measurements of APOBEC3G Provide Structural Basis for Binding of Single-Stranded DNA and Processivity Viruses 14(9):1974 (2022)
Barzak F, Ryan T, Mohammadzadeh N, Harjes S, Kvach M, Kurup H, Krause K, Chelico L, Filichev V, Harjes E, Jameson G
RgGuinier 4.2 nm
Dmax 13.3 nm
VolumePorod 350 nm3

SASDMZ6 – single-stranded DNA dC->dU-editing enzyme APOBEC3G full length in complex with DNA: tetramer

DNA dC->dU-editing enzyme APOBEC-3G40-mer single stranded inhibitory DNA experimental SAS data
DAMFILT model
Sample: DNA dC->dU-editing enzyme APOBEC-3G tetramer, 186 kDa Homo sapiens protein
40-mer single stranded inhibitory DNA dimer, 24 kDa DNA
Buffer: 50 mM phosphate pH 6.0, 200 mM NaCl, 2 mM β-mercaptoethanol (β-ME), 5% glycerol, 200 µM Na2-EDTA, pH: 6
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Aug 6
Small-Angle X-ray Scattering (SAXS) Measurements of APOBEC3G Provide Structural Basis for Binding of Single-Stranded DNA and Processivity Viruses 14(9):1974 (2022)
Barzak F, Ryan T, Mohammadzadeh N, Harjes S, Kvach M, Kurup H, Krause K, Chelico L, Filichev V, Harjes E, Jameson G
RgGuinier 4.7 nm
Dmax 16.2 nm
VolumePorod 395 nm3

SASDM27 – single-stranded DNA dC->dU-editing enzyme APOBEC3G full length in complex with DNA: monomer

40-mer single stranded inhibitory DNADNA dC->dU-editing enzyme APOBEC-3G experimental SAS data
DAMFILT model
Sample: 40-mer single stranded inhibitory DNA monomer, 12 kDa DNA
DNA dC->dU-editing enzyme APOBEC-3G monomer, 46 kDa Homo sapiens protein
Buffer: 50 mM phosphate pH 6.0, 200 mM NaCl, 2 mM β-mercaptoethanol (β-ME), 5% glycerol, 200 µM Na2-EDTA, pH: 6
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Aug 6
Small-Angle X-ray Scattering (SAXS) Measurements of APOBEC3G Provide Structural Basis for Binding of Single-Stranded DNA and Processivity Viruses 14(9):1974 (2022)
Barzak F, Ryan T, Mohammadzadeh N, Harjes S, Kvach M, Kurup H, Krause K, Chelico L, Filichev V, Harjes E, Jameson G
RgGuinier 3.1 nm
Dmax 10.0 nm
VolumePorod 118 nm3

SASDMX7 – Human histone deacetylase 6

Histone deacetylase 6 experimental SAS data
Human histone deacetylase 6 Rg histogram
Sample: Histone deacetylase 6 monomer, 131 kDa Homo sapiens protein
Buffer: 30 mM HEPES, 140 mM NaCl, 10 mM KCl, 0.25 mM TCEP, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Dec 10
In-solution structure and oligomerization of human histone deacetylase 6 - an integrative approach. FEBS J (2022)
Shukla S, Komarek J, Novakova Z, Nedvedova J, Ustinova K, Vankova P, Kadek A, Uetrecht C, Mertens H, Barinka C
RgGuinier 7.0 nm
Dmax 26.0 nm
VolumePorod 316 nm3

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, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB
RgGuinier 2.4 nm
Dmax 7.4 nm
VolumePorod 66 nm3