Browse by MACROMOLECULE type: protein

SASDLM7 – Bartonella effector protein (Bep1), 35 °C

Bartonella effector protein (Bep) substrate of VirB T4SS experimental SAS data
GASBOR model
Sample: Bartonella effector protein (Bep) substrate of VirB T4SS monomer, 64 kDa Bartonella clarridgeiae (strain … protein
Buffer: 25 mM Hepes, 300 mM NaCl, 1 mM TCEP, 5% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Jun 26
Structure and function of Bartonella effector protein 1: target and interdomain interactions University of Basel PhD thesis 15051 (2023)
Markus Huber, Jens Reiners
RgGuinier 4.1 nm
Dmax 14.4 nm
VolumePorod 108 nm3

SASDRE6 – Ras GTPase-activating protein 1 (p120RasGAP, amino acids 174–1047)

Ras GTPase-activating protein 1 experimental SAS data
ALPHAFOLD model
Sample: Ras GTPase-activating protein 1 monomer, 101 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Nov 4
Diverse p120RasGAP interactions with doubly phosphorylated partners EphB4, p190RhoGAP and Dok1 Journal of Biological Chemistry :105098 (2023)
Vish K, Stiegler A, Boggon T
RgGuinier 4.0 nm
Dmax 14.0 nm
VolumePorod 172 nm3

SASDRF6 – Ras GTPase-activating protein 1 (p120RasGAP, amino acids 174–1047) bound to doubly phosphorylated EphB4 peptide

Ephrin type-B receptor 4Ras GTPase-activating protein 1 experimental SAS data
Ephrin type-B receptor 4 Ras GTPase-activating protein 1 Kratky plot
Sample: Ephrin type-B receptor 4 monomer, 2 kDa Homo sapiens protein
Ras GTPase-activating protein 1 monomer, 101 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Nov 4
Diverse p120RasGAP interactions with doubly phosphorylated partners EphB4, p190RhoGAP and Dok1 Journal of Biological Chemistry :105098 (2023)
Vish K, Stiegler A, Boggon T
RgGuinier 3.9 nm
Dmax 13.7 nm
VolumePorod 176 nm3

SASDRG6 – Ras GTPase-activating protein 1 (p120RasGAP, amino acids 174–1047) bound to doubly phosphorylated p190RhoGAP peptide

Rho GTPase-activating protein 35Ras GTPase-activating protein 1 experimental SAS data
Rho GTPase-activating protein 35 Ras GTPase-activating protein 1 Kratky plot
Sample: Rho GTPase-activating protein 35 monomer, 3 kDa Homo sapiens protein
Ras GTPase-activating protein 1 monomer, 101 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Nov 4
Diverse p120RasGAP interactions with doubly phosphorylated partners EphB4, p190RhoGAP and Dok1 Journal of Biological Chemistry :105098 (2023)
Vish K, Stiegler A, Boggon T
RgGuinier 4.0 nm
Dmax 15.1 nm
VolumePorod 194 nm3

SASDRH6 – Ras GTPase-activating protein 1 (p120RasGAP, amino acids 174–1047) bound to a doubly phosphorylated Dok1 peptide

Ras GTPase-activating protein 1Docking protein 1 experimental SAS data
Ras GTPase-activating protein 1 Docking protein 1 Kratky plot
Sample: Ras GTPase-activating protein 1 monomer, 101 kDa Homo sapiens protein
Docking protein 1 monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Nov 4
Diverse p120RasGAP interactions with doubly phosphorylated partners EphB4, p190RhoGAP and Dok1 Journal of Biological Chemistry :105098 (2023)
Vish K, Stiegler A, Boggon T
RgGuinier 4.0 nm
Dmax 14.6 nm
VolumePorod 196 nm3

SASDRJ6 – SH2-SH3-SH2 domains of Ras GTPase-activating protein 1 (p120RasGAP)

Ras GTPase-activating protein 1 (C236S, C261S, C372S, C402S) experimental SAS data
Ras GTPase-activating protein 1 (C236S, C261S, C372S, C402S) Kratky plot
Sample: Ras GTPase-activating protein 1 (C236S, C261S, C372S, C402S) monomer, 31 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8, 350 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Dec 12
Diverse p120RasGAP interactions with doubly phosphorylated partners EphB4, p190RhoGAP and Dok1 Journal of Biological Chemistry :105098 (2023)
Vish K, Stiegler A, Boggon T
RgGuinier 2.5 nm
Dmax 9.8 nm
VolumePorod 42 nm3

SASDRK6 – SH2-SH3-SH2 domains of Ras GTPase-activating protein 1 (p120RasGAP) bound to a doubly phosphorylated EphB4 peptide

Ephrin type-B receptor 4Ras GTPase-activating protein 1 (C236S, C261S, C372S, C402S) experimental SAS data
Ephrin type-B receptor 4 Ras GTPase-activating protein 1 (C236S, C261S, C372S, C402S) Kratky plot
Sample: Ephrin type-B receptor 4 monomer, 2 kDa Homo sapiens protein
Ras GTPase-activating protein 1 (C236S, C261S, C372S, C402S) monomer, 31 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8, 350 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Dec 12
Diverse p120RasGAP interactions with doubly phosphorylated partners EphB4, p190RhoGAP and Dok1 Journal of Biological Chemistry :105098 (2023)
Vish K, Stiegler A, Boggon T
RgGuinier 2.7 nm
Dmax 10.5 nm
VolumePorod 44 nm3

SASDRL6 – SH2-SH3-SH2 domains of Ras GTPase-activating protein 1 (p120RasGAP) bound to a doubly phosphorylated p190RhoGAP peptide

Rho GTPase-activating protein 35Ras GTPase-activating protein 1 (C236S, C261S, C372S, C402S) experimental SAS data
Rho GTPase-activating protein 35 Ras GTPase-activating protein 1 (C236S, C261S, C372S, C402S) Kratky plot
Sample: Rho GTPase-activating protein 35 monomer, 3 kDa Homo sapiens protein
Ras GTPase-activating protein 1 (C236S, C261S, C372S, C402S) monomer, 31 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8, 350 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Dec 12
Diverse p120RasGAP interactions with doubly phosphorylated partners EphB4, p190RhoGAP and Dok1 Journal of Biological Chemistry :105098 (2023)
Vish K, Stiegler A, Boggon T
RgGuinier 2.4 nm
Dmax 7.7 nm
VolumePorod 44 nm3

SASDRR8 – Сhloroplast FOF1-ATP synthase from Spinacia oleracea purified by anion-exchange chromatography (~ 300 mM NaCl)

ATP synthase subunit alpha, chloroplasticATP synthase subunit beta, chloroplasticATP synthase gamma chain, chloroplasticATP synthase delta chain, chloroplasticATP synthase epsilon chain, chloroplasticATP synthase subunit a, chloroplasticATP synthase subunit b, chloroplasticATP synthase subunit b', chloroplasticATP synthase subunit c, chloroplastic4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside experimental SAS data
MEMPROT model
Sample: ATP synthase subunit alpha, chloroplastic trimer, 166 kDa Spinacia oleracea protein
ATP synthase subunit beta, chloroplastic trimer, 161 kDa Spinacia oleracea protein
ATP synthase gamma chain, chloroplastic monomer, 40 kDa Spinacia oleracea protein
ATP synthase delta chain, chloroplastic monomer, 28 kDa Spinacia oleracea protein
ATP synthase epsilon chain, chloroplastic monomer, 15 kDa Spinacia oleracea protein
ATP synthase subunit a, chloroplastic monomer, 27 kDa Spinacia oleracea protein
ATP synthase subunit b, chloroplastic monomer, 21 kDa Spinacia oleracea protein
ATP synthase subunit b', chloroplastic monomer, 24 kDa Spinacia oleracea protein
ATP synthase subunit c, chloroplastic 14-mer, 112 kDa Spinacia oleracea protein
4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside 0, 283 kDa
Buffer: 300 mM NaCl, 30 mM HEPES, 2 mM MgCl2, 0.04% (w/v) tPCC-α-M, pH: 8
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2020 Oct 3
I-Shaped Dimers of a Plant Chloroplast FOF1-ATP Synthase in Response to Changes in Ionic Strength International Journal of Molecular Sciences 24(13):10720 (2023)
Osipov S, Ryzhykau Y, Zinovev E, Minaeva A, Ivashchenko S, Verteletskiy D, Sudarev V, Kuklina D, Nikolaev M, Semenov Y, Zagryadskaya Y, Okhrimenko I, Gette M, Dronova E, Shishkin A, Dencher N, Kuklin A, Ivanovich V, Uversky V, Vlasov A
RgGuinier 6.6 nm
Dmax 27.5 nm
VolumePorod 927 nm3

SASDRS8 – Сhloroplast FOF1-ATP synthase from Spinacia oleracea at 150 mM NaCl

ATP synthase subunit alpha, chloroplasticATP synthase subunit beta, chloroplasticATP synthase gamma chain, chloroplasticATP synthase delta chain, chloroplasticATP synthase epsilon chain, chloroplasticATP synthase subunit a, chloroplasticATP synthase subunit b, chloroplasticATP synthase subunit b', chloroplasticATP synthase subunit c, chloroplastic4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside experimental SAS data
OTHER [STATIC IMAGE] model
Sample: ATP synthase subunit alpha, chloroplastic trimer, 166 kDa Spinacia oleracea protein
ATP synthase subunit beta, chloroplastic trimer, 161 kDa Spinacia oleracea protein
ATP synthase gamma chain, chloroplastic monomer, 40 kDa Spinacia oleracea protein
ATP synthase delta chain, chloroplastic monomer, 28 kDa Spinacia oleracea protein
ATP synthase epsilon chain, chloroplastic monomer, 15 kDa Spinacia oleracea protein
ATP synthase subunit a, chloroplastic monomer, 27 kDa Spinacia oleracea protein
ATP synthase subunit b, chloroplastic monomer, 21 kDa Spinacia oleracea protein
ATP synthase subunit b', chloroplastic monomer, 24 kDa Spinacia oleracea protein
ATP synthase subunit c, chloroplastic 14-mer, 112 kDa Spinacia oleracea protein
4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside 0, 283 kDa
Buffer: 150 mM NaCl, 30 mM HEPES, 2 mM MgCl2, 0.04% (w/v) tPCC-α-M, pH: 8
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2020 Oct 3
I-Shaped Dimers of a Plant Chloroplast FOF1-ATP Synthase in Response to Changes in Ionic Strength International Journal of Molecular Sciences 24(13):10720 (2023)
Osipov S, Ryzhykau Y, Zinovev E, Minaeva A, Ivashchenko S, Verteletskiy D, Sudarev V, Kuklina D, Nikolaev M, Semenov Y, Zagryadskaya Y, Okhrimenko I, Gette M, Dronova E, Shishkin A, Dencher N, Kuklin A, Ivanovich V, Uversky V, Vlasov A
RgGuinier 9.6 nm
Dmax 41.5 nm
VolumePorod 1506 nm3