Browse by MODEL: No model

SASDDC8 – Periplasmic domain of inner membrane protein GspL, tetramer

Type II secretion system protein L, periplasmic domain experimental SAS data
Type II secretion system protein L, periplasmic domain Kratky plot
Sample: Type II secretion system protein L, periplasmic domain dimer, 28 kDa Pseudomonas aeruginosa protein
Buffer: 50 mM TRIS, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2016 Apr 8
Structure and oligomerization of the periplasmic domain of GspL from the type II secretion system of Pseudomonas aeruginosa. Sci Rep 8(1):16760 (2018)
Fulara A, Vandenberghe I, Read RJ, Devreese B, Savvides SN
RgGuinier 3.2 nm
Dmax 10.5 nm

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

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

SASDEF3 – Paenibacillus xanthan lyase (PXL) at 4 °C

Paenibacillus xanthan lyase experimental SAS data
Paenibacillus xanthan lyase Kratky plot
Sample: Paenibacillus xanthan lyase monomer, 113 kDa Paenibacillus sp-62047 protein
Buffer: 20 mM Tris,, pH: 8.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Dec 15
Structure and Dynamics of a Promiscuous Xanthan Lyase from Paenibacillus nanensis and the Design of Variants with Increased Stability and Activity. Cell Chem Biol 26(2):191-202.e6 (2019)
Jensen PF, Kadziola A, Comamala G, Segura DR, Anderson L, Poulsen JN, Rasmussen KK, Agarwal S, Sainathan RK, Monrad RN, Svendsen A, Nielsen JE, Lo Leggio L, Rand KD
RgGuinier 3.7 nm
Dmax 13.1 nm
VolumePorod 137 nm3

SASDEG3 – Paenibacillus xanthan lyase (PXL) at 20 °C

Paenibacillus xanthan lyase experimental SAS data
Paenibacillus xanthan lyase Kratky plot
Sample: Paenibacillus xanthan lyase monomer, 113 kDa Paenibacillus sp-62047 protein
Buffer: 20 mM Tris,, pH: 8.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Dec 15
Structure and Dynamics of a Promiscuous Xanthan Lyase from Paenibacillus nanensis and the Design of Variants with Increased Stability and Activity. Cell Chem Biol 26(2):191-202.e6 (2019)
Jensen PF, Kadziola A, Comamala G, Segura DR, Anderson L, Poulsen JN, Rasmussen KK, Agarwal S, Sainathan RK, Monrad RN, Svendsen A, Nielsen JE, Lo Leggio L, Rand KD
RgGuinier 3.8 nm
Dmax 13.8 nm
VolumePorod 134 nm3

SASDDS8 – Neural/ectodermal development factor IMP-L2

Neural/ectodermal development factor IMP-L2 experimental SAS data
Neural/ectodermal development factor IMP-L2 Kratky plot
Sample: Neural/ectodermal development factor IMP-L2 dimer, 60 kDa Drosophila melanogaster protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at ID14-3, ESRF on 2011 Nov 20
Structures of insect Imp-L2 suggest an alternative strategy for regulating the bioavailability of insulin-like hormones. Nat Commun 9(1):3860 (2018)
Roed NK, Viola CM, Kristensen O, Schluckebier G, Norrman M, Sajid W, Wade JD, Andersen AS, Kristensen C, Ganderton TR, Turkenburg JP, De Meyts P, Brzozowski AM
RgGuinier 3.1 nm
Dmax 12.0 nm
VolumePorod 93 nm3

SASDDT8 – Neural/ectodermal development factor IMP-L2 in complex with insulin-like peptide 5 (DILP5)

Insulin-like peptide 5Neural/ectodermal development factor IMP-L2 experimental SAS data
Insulin-like peptide 5 Neural/ectodermal development factor IMP-L2 Kratky plot
Sample: Insulin-like peptide 5 monomer, 5 kDa Drosophila melanogaster protein
Neural/ectodermal development factor IMP-L2 monomer, 30 kDa Drosophila melanogaster protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at ID14-3, ESRF on 2011 Nov 20
Structures of insect Imp-L2 suggest an alternative strategy for regulating the bioavailability of insulin-like hormones. Nat Commun 9(1):3860 (2018)
Roed NK, Viola CM, Kristensen O, Schluckebier G, Norrman M, Sajid W, Wade JD, Andersen AS, Kristensen C, Ganderton TR, Turkenburg JP, De Meyts P, Brzozowski AM
RgGuinier 2.6 nm
Dmax 9.0 nm
VolumePorod 55 nm3

SASDDT3 – p-hydroxyphenylacetate 3-hydroxylase, reductase component: 2 mg/ml of wild-type C1 in the absence of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase, reductase component experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase, reductase component Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase, reductase component dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, and 5% glycerol, pH: 7
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2017 Mar 7
Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands. Arch Biochem Biophys 653:24-38 (2018)
Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D
RgGuinier 2.4 nm
Dmax 6.9 nm
VolumePorod 94 nm3