Browse by MACROMOLECULE type: protein

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

SASDRT8 – Сhloroplast FOF1-ATP synthase from Spinacia oleracea at 250 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: 250 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 7.4 nm
Dmax 33.0 nm
VolumePorod 949 nm3

SASDRU8 – Сhloroplast FOF1-ATP synthase from Spinacia oleracea at 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
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: 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 7.8 nm
Dmax 39.5 nm
VolumePorod 1127 nm3

SASDRV8 – Сhloroplast FOF1-ATP synthase from Spinacia oleracea at 350 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: 350 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 8.9 nm
Dmax 44.5 nm
VolumePorod 1150 nm3

SASDRW8 – Сhloroplast FOF1-ATP synthase from Spinacia oleracea at 450 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: 450 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 10.8 nm
Dmax 46.5 nm
VolumePorod 1703 nm3

SASDDD6 – Human Guanylate-binding protein (hGBP1)

Guanylate-binding protein 1 experimental SAS data
DAMMIF model
Sample: Guanylate-binding protein 1 monomer, 68 kDa Homo sapiens protein
Buffer: 50 mM TRIS, 5 mM MgCl2, 150 mM NaCl, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2018 Apr 30
Integrative dynamic structural biology unveils conformers essential for the oligomerization of a large GTPase. Elife 12 (2023)
Peulen TO, Hengstenberg CS, Biehl R, Dimura M, Lorenz C, Valeri A, Folz J, Hanke CA, Ince S, Vöpel T, Farago B, Gohlke H, Klare JP, Stadler AM, Seidel CAM, Herrmann C
RgGuinier 3.9 nm
Dmax 14.4 nm
VolumePorod 105 nm3

SASDRN5 – Nucleolar RNA Chaperone-Like Protein 1 (NURC1)

AT5g04600/T32M21_200 experimental SAS data
GASBOR model
Sample: AT5g04600/T32M21_200 monomer, 25 kDa Arabidopsis thaliana protein
Buffer: 50 mM HNa2PO4, 300 mM NaCl, 5% glycerol (v/v), 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Jun 22
Structural and functional analysis of a plant nucleolar RNA chaperone-like protein. Sci Rep 13(1):9656 (2023)
Fernandes R, Ostendorp A, Ostendorp S, Mehrmann J, Falke S, Graewert MA, Weingartner M, Kehr J, Hoth S
RgGuinier 3.5 nm
Dmax 12.4 nm
VolumePorod 66 nm3

SASDNJ5 – Full length 3-phosphoinositide-dependent protein kinase (PDK1)

3-phosphoinositide-dependent protein kinase 1 experimental SAS data
DAMMIF model
Sample: 3-phosphoinositide-dependent protein kinase 1 monomer, 65 kDa Homo sapiens protein
Buffer: 20 mM Tris-HCl pH 7.4, 250 mM NaCl, 1 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Mar 26
Modulation of the substrate specificity of the kinase PDK1 by distinct conformations of the full-length protein Science Signaling 16(789) (2023)
Sacerdoti M, Gross L, Riley A, Zehnder K, Ghode A, Klinke S, Anand G, Paris K, Winkel A, Herbrand A, Godage H, Cozier G, Süß E, Schulze J, Pastor-Flores D, Bollini M, Cappellari M, Svergun D, Gräwert M, Aramendia P, Leroux A, Potter B, Camacho C, Biondi R
RgGuinier 3.5 nm
Dmax 11.2 nm
VolumePorod 107 nm3

SASDNK5 – Full length 3-phosphoinositide-dependent protein kinase (PDK1) in the presence of HYG8 (2-O-benzoyl-Ins(1,3,4,5,6)P5)

3-phosphoinositide-dependent protein kinase 12-O-benzoyl-Ins(1,3,4,5,6)P5 experimental SAS data
DAMMIF model
Sample: 3-phosphoinositide-dependent protein kinase 1 monomer, 65 kDa Homo sapiens protein
2-O-benzoyl-Ins(1,3,4,5,6)P5 monomer, 1 kDa synthetic construct
Buffer: 20 mM Tris-HCl pH 7.4, 250 mM NaCl, 1 mM DTT, 1 μM HYG8, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Mar 26
Modulation of the substrate specificity of the kinase PDK1 by distinct conformations of the full-length protein Science Signaling 16(789) (2023)
Sacerdoti M, Gross L, Riley A, Zehnder K, Ghode A, Klinke S, Anand G, Paris K, Winkel A, Herbrand A, Godage H, Cozier G, Süß E, Schulze J, Pastor-Flores D, Bollini M, Cappellari M, Svergun D, Gräwert M, Aramendia P, Leroux A, Potter B, Camacho C, Biondi R
RgGuinier 3.5 nm
Dmax 11.5 nm
VolumePorod 98 nm3

SASDNL5 – Double mutant catalytic domain of 3-phosphoinositide-dependent protein kinase 1 (PDK1 50–359; Y188G Q292A)

3-phosphoinositide-dependent protein kinase 1 (Y188G Q292A) experimental SAS data
SREFLEX model
Sample: 3-phosphoinositide-dependent protein kinase 1 (Y188G Q292A) monomer, 35 kDa Homo sapiens protein
Buffer: 20 mM Tris-HCl pH 7.4, 250 mM NaCl, 1 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Mar 26
Modulation of the substrate specificity of the kinase PDK1 by distinct conformations of the full-length protein Science Signaling 16(789) (2023)
Sacerdoti M, Gross L, Riley A, Zehnder K, Ghode A, Klinke S, Anand G, Paris K, Winkel A, Herbrand A, Godage H, Cozier G, Süß E, Schulze J, Pastor-Flores D, Bollini M, Cappellari M, Svergun D, Gräwert M, Aramendia P, Leroux A, Potter B, Camacho C, Biondi R
RgGuinier 2.4 nm
Dmax 7.0 nm
VolumePorod 57 nm3