Browse by ORGANISM: Escherichia coli

SASDKN7 – Sulfite reductase flavoprotein-60-ΔAAPSQS

Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) experimental SAS data
Sample: Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) monomer, 61 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at EQ-SANS (BL-6), Spallation Neutron Source on 2018 Jul 11
NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation unique to this diflavin reductase Journal of Structural Biology 205(2):170-179 (2019)
Tavolieri A, Murray D, Askenasy I, Pennington J, McGarry L, Stanley C, Stroupe M
RgGuinier 3.2 nm
Dmax 11.3 nm
VolumePorod 73 nm3

SASDES4 – ACA8 in stealth nanodisc (SANS, 100% D2O)

Membrane scaffold protein 1D1 (deuterated, 75%)1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)Calcium-transporting ATPase 8, plasma membrane-type experimental SAS data
Membrane scaffold protein 1D1 (deuterated, 75%) 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) Calcium-transporting ATPase 8, plasma membrane-type Kratky plot
Sample: Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein
1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl), 1 kDa Escherichia coli
Calcium-transporting ATPase 8, plasma membrane-type monomer, 118 kDa Arabidopsis thaliana protein
Buffer: 30 mM Tris, 150 mM NaCl, 1mM MgCl2, 1 mM CaCl2, pH: 7.5
Experiment: SANS data collected at SANS-1, Heinz Maier-Leibnitz Zentrum on 2017 Aug 28
Structural basis for activation of plasma-membrane Ca2+-ATPase by calmodulin. Commun Biol 1:206 (2018)
Nitsche J, Josts I, Heidemann J, Mertens HD, Maric S, Moulin M, Haertlein M, Busch S, Forsyth VT, Svergun DI, Uetrecht C, Tidow H
RgGuinier 4.0 nm
Dmax 13.0 nm
VolumePorod 202 nm3

SASDET4 – ACA8 complex with Calmodulin (75% deuterated) in stealth nanodisc (SANS, 100% D2O)

Membrane scaffold protein 1D1 (deuterated, 75%)1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)Calcium-transporting ATPase 8, plasma membrane-typeCalmodulin-7 (deuterated 75%) experimental SAS data
ACA8 complex with Calmodulin (75% deuterated) in stealth nanodisc (SANS, 100% D2O) Rg histogram
Sample: Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein
1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl), 1 kDa Escherichia coli
Calcium-transporting ATPase 8, plasma membrane-type monomer, 118 kDa Arabidopsis thaliana protein
Calmodulin-7 (deuterated 75%) monomer, Arabidopsis thaliana protein
Buffer: 30 mM Tris, 150 mM NaCl, 1mM MgCl2, 1 mM CaCl2, pH: 7.5
Experiment: SANS data collected at SANS-1, Heinz Maier-Leibnitz Zentrum on 2017 Aug 28
Structural basis for activation of plasma-membrane Ca2+-ATPase by calmodulin. Commun Biol 1:206 (2018)
Nitsche J, Josts I, Heidemann J, Mertens HD, Maric S, Moulin M, Haertlein M, Busch S, Forsyth VT, Svergun DI, Uetrecht C, Tidow H
RgGuinier 4.3 nm
Dmax 15.0 nm
VolumePorod 217 nm3

SASDEU4 – ACA8 complex with Calmodulin (hydrogenated) in stealth nanodisc (SANS, 100% D2O)

Membrane scaffold protein 1D1 (deuterated, 75%)1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)Calcium-transporting ATPase 8, plasma membrane-typeCalmodulin-7 experimental SAS data
Membrane scaffold protein 1D1 (deuterated, 75%) 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) Calcium-transporting ATPase 8, plasma membrane-type Calmodulin-7 Kratky plot
Sample: Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein
1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl), 1 kDa Escherichia coli
Calcium-transporting ATPase 8, plasma membrane-type monomer, 118 kDa Arabidopsis thaliana protein
Calmodulin-7 monomer, Arabidopsis thaliana protein
Buffer: 30 mM Tris, 150 mM NaCl, 1mM MgCl2, 1 mM CaCl2, pH: 7.5
Experiment: SANS data collected at SANS-1, Heinz Maier-Leibnitz Zentrum on 2017 Aug 28
Structural basis for activation of plasma-membrane Ca2+-ATPase by calmodulin. Commun Biol 1:206 (2018)
Nitsche J, Josts I, Heidemann J, Mertens HD, Maric S, Moulin M, Haertlein M, Busch S, Forsyth VT, Svergun DI, Uetrecht C, Tidow H
RgGuinier 4.8 nm
Dmax 18.0 nm
VolumePorod 297 nm3

SASDEV4 – ACA8 protein (apo) in stealth nanodisc

Membrane scaffold protein 1D1 (deuterated, 75%)1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)Calcium-transporting ATPase 8, plasma membrane-type experimental SAS data
Membrane scaffold protein 1D1 (deuterated, 75%) 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) Calcium-transporting ATPase 8, plasma membrane-type Kratky plot
Sample: Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein
1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl), 1 kDa Escherichia coli
Calcium-transporting ATPase 8, plasma membrane-type monomer, 118 kDa Arabidopsis thaliana protein
Buffer: 30 mM Tris, 150 mM NaCl, 1mM MgCl2, 1 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 8
Structural basis for activation of plasma-membrane Ca2+-ATPase by calmodulin. Commun Biol 1:206 (2018)
Nitsche J, Josts I, Heidemann J, Mertens HD, Maric S, Moulin M, Haertlein M, Busch S, Forsyth VT, Svergun DI, Uetrecht C, Tidow H
RgGuinier 5.3 nm
Dmax 20.0 nm
VolumePorod 626 nm3

SASDEW4 – ACA8 complex with Calmodulin (hydrogenated) in stealth nanodisc

Membrane scaffold protein 1D1 (deuterated, 75%)1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)Calcium-transporting ATPase 8, plasma membrane-typeCalmodulin-7 experimental SAS data
Membrane scaffold protein 1D1 (deuterated, 75%) 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) Calcium-transporting ATPase 8, plasma membrane-type Calmodulin-7 Kratky plot
Sample: Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein
1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl), 1 kDa Escherichia coli
Calcium-transporting ATPase 8, plasma membrane-type monomer, 118 kDa Arabidopsis thaliana protein
Calmodulin-7 monomer, Arabidopsis thaliana protein
Buffer: 30 mM Tris, 150 mM NaCl, 1mM MgCl2, 1 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 8
Structural basis for activation of plasma-membrane Ca2+-ATPase by calmodulin. Commun Biol 1:206 (2018)
Nitsche J, Josts I, Heidemann J, Mertens HD, Maric S, Moulin M, Haertlein M, Busch S, Forsyth VT, Svergun DI, Uetrecht C, Tidow H
RgGuinier 5.9 nm
Dmax 22.0 nm
VolumePorod 805 nm3

SASDJW2 – Modification dependent EcoKMcrA restriction endonuclease

5-methylcytosine-specific restriction enzyme A experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: 5-methylcytosine-specific restriction enzyme A dimer, 65 kDa Escherichia coli protein
Buffer: 20 mM Tris–HCl pH 7.5, 200 mM KCl, 0.1 mM EDTA, 0.01% (w/v) sodium azide and 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 May 24
Activity and structure of EcoKMcrA. Nucleic Acids Res 46(18):9829-9841 (2018)
Czapinska H, Kowalska M, Zagorskaite E, Manakova E, Slyvka A, Xu SY, Siksnys V, Sasnauskas G, Bochtler M
RgGuinier 3.7 nm
Dmax 13.0 nm
VolumePorod 95 nm3

SASDJX2 – Modification dependent EcoKMcrA restriction endonuclease in complex with cognate hemimethylated 12bp oligoduplex

cognate hemimethylated 12-bp oligoduplex5-methylcytosine-specific restriction enzyme A experimental SAS data
SASREF model
Sample: Cognate hemimethylated 12-bp oligoduplex dimer, 15 kDa DNA
5-methylcytosine-specific restriction enzyme A dimer, 65 kDa Escherichia coli protein
Buffer: 20 mM Tris–HCl pH 7.5, 200 mM KCl, 0.1 mM EDTA, 0.01% (w/v) sodium azide and 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 May 24
Activity and structure of EcoKMcrA. Nucleic Acids Res 46(18):9829-9841 (2018)
Czapinska H, Kowalska M, Zagorskaite E, Manakova E, Slyvka A, Xu SY, Siksnys V, Sasnauskas G, Bochtler M
RgGuinier 3.9 nm
Dmax 13.5 nm
VolumePorod 69 nm3

SASDJY2 – N-terminal domain of modification dependent EcoKMcrA restriction endonuclease

5-methylcytosine-specific restriction enzyme A (N-terminal domain) experimental SAS data
OTHER model
Sample: 5-methylcytosine-specific restriction enzyme A (N-terminal domain) monomer, 21 kDa Escherichia coli protein
Buffer: 20 mM Tris–HCl pH 7.5, 200 mM KCl, 0.1 mM EDTA, 0.01% (w/v) sodium azide, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 May 24
Activity and structure of EcoKMcrA. Nucleic Acids Res 46(18):9829-9841 (2018)
Czapinska H, Kowalska M, Zagorskaite E, Manakova E, Slyvka A, Xu SY, Siksnys V, Sasnauskas G, Bochtler M
RgGuinier 2.1 nm
Dmax 7.5 nm
VolumePorod 29 nm3

SASDJZ2 – N-terminal domain of modification dependent EcoKMcrA restriction endonuclease in complex with cognate hemimethylated 12bp oligoduplex

5-methylcytosine-specific restriction enzyme A (N-terminal domain)cognate hemimethylated 12-bp oligoduplex experimental SAS data
OTHER model
Sample: 5-methylcytosine-specific restriction enzyme A (N-terminal domain) monomer, 21 kDa Escherichia coli protein
Cognate hemimethylated 12-bp oligoduplex monomer, 7 kDa DNA
Buffer: 20 mM Tris–HCl pH 7.5, 200 mM KCl, 0.1 mM EDTA, 0.01% (w/v) sodium azide and 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 May 24
Activity and structure of EcoKMcrA. Nucleic Acids Res 46(18):9829-9841 (2018)
Czapinska H, Kowalska M, Zagorskaite E, Manakova E, Slyvka A, Xu SY, Siksnys V, Sasnauskas G, Bochtler M
RgGuinier 2.1 nm
Dmax 7.5 nm
VolumePorod 29 nm3