Browse by ORGANISM: other species

SASDQW7 – Bicelles formed by POPC POPG and cholate

Cholate - 3α,7α,12α-trihydroxy-5β-cholan-24-oic acidPOPC - 2-oleoyl-1-palmitoyl-sn-glyecro-3-phosphocholinePOPG - 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1′-rac-glycerol) experimental SAS data
Cholate - 3α,7α,12α-trihydroxy-5β-cholan-24-oic acid POPC - 2-oleoyl-1-palmitoyl-sn-glyecro-3-phosphocholine POPG - 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1′-rac-glycerol) Kratky plot
Sample: Cholate - 3α,7α,12α-trihydroxy-5β-cholan-24-oic acid None, lipid
POPC - 2-oleoyl-1-palmitoyl-sn-glyecro-3-phosphocholine None, lipid
POPG - 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1′-rac-glycerol) None, lipid
Buffer: Tris buffered saline, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Mar 17
Expanding the Toolbox for Bicelle-Forming Surfactant–Lipid Mixtures Molecules 27(21):7628 (2022)
Giudice R, Paracini N, Laursen T, Blanchet C, Roosen-Runge F, Cárdenas M

SASDQX7 – Bicelles formed by POPC POPG and DHPC

DHPC - 1,2-dihexanoyl-sn-glycero-3-phosphocholinePOPC - 2-oleoyl-1-palmitoyl-sn-glyecro-3-phosphocholinePOPG - 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1′-rac-glycerol) experimental SAS data
DHPC - 1,2-dihexanoyl-sn-glycero-3-phosphocholine POPC - 2-oleoyl-1-palmitoyl-sn-glyecro-3-phosphocholine POPG - 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1′-rac-glycerol) Kratky plot
Sample: DHPC - 1,2-dihexanoyl-sn-glycero-3-phosphocholine None, lipid
POPC - 2-oleoyl-1-palmitoyl-sn-glyecro-3-phosphocholine None, lipid
POPG - 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1′-rac-glycerol) None, lipid
Buffer: Tris buffered saline, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Mar 17
Expanding the Toolbox for Bicelle-Forming Surfactant–Lipid Mixtures Molecules 27(21):7628 (2022)
Giudice R, Paracini N, Laursen T, Blanchet C, Roosen-Runge F, Cárdenas M

SASDP46 – Glycoside Hydrolase Family 5 endo-mannanase retrieved from Capybara gut metagenome

GH5 endo-mannanase from Capybara gut metagenome experimental SAS data
PYMOL model
Sample: GH5 endo-mannanase from Capybara gut metagenome monomer, 46 kDa metagenome protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2018 Oct 30
Glycoside hydrolase subfamily GH5_57 features a highly redesigned catalytic interface to process complex hetero-β-mannans. Acta Crystallogr D Struct Biol 78(Pt 11):1358-1372 (2022)
Martins MP, Morais MAB, Persinoti GF, Galinari RH, Yu L, Yoshimi Y, Passos Nunes FB, Lima TB, Barbieri SF, Silveira JLM, Lombard V, Terrapon N, Dupree P, Henrissat B, Murakami MT
RgGuinier 2.3 nm
Dmax 5.5 nm
VolumePorod 58 nm3

SASDQG6 – N-terminal truncation mutant of the periplasmic region of conjugal transfer mating pair stabilization protein TraG* from the R100 plasmid

Conjugal transfer mating pair stabilization protein TraG experimental SAS data
DAMMIF model
Sample: Conjugal transfer mating pair stabilization protein TraG monomer, 52 kDa Shigella flexneri 4c protein
Buffer: 20 mM HEPES, 100 mM NaCl, 5% glycerol, pH: 7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Feb 23
Solution characterization of the dynamic conjugative entry exclusion protein TraG Structural Dynamics 9(6):064702 (2022)
Bragagnolo N, Audette G
RgGuinier 4.1 nm
Dmax 17.5 nm
VolumePorod 130 nm3

SASDQH6 – Periplasmic region of the conjugal transfer mating pair stabilization protein TraG* from the R100 plasmid

Conjugal transfer mating pair stabilization protein TraG experimental SAS data
DAMMIF model
Sample: Conjugal transfer mating pair stabilization protein TraG monomer, 57 kDa Shigella flexneri 4c protein
Buffer: 20 mM HEPES, 100 mM NaCl, 5% glycerol, 0.05% NP40, pH: 7
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Feb 23
Solution characterization of the dynamic conjugative entry exclusion protein TraG Structural Dynamics 9(6):064702 (2022)
Bragagnolo N, Audette G
RgGuinier 5.8 nm
Dmax 45.0 nm

SASDQN5 – Candida glabrata Metacaspase in 10 mM CaCl2

Metacaspase-1 experimental SAS data
Metacaspase-1 Kratky plot
Sample: Metacaspase-1 monomer, 46 kDa Candida glabrata (strain … protein
Buffer: 10 mM HEPES, 150 mM NaCl, 1% glycerol, 10 mM CaCl2, pH: 7.6
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Sep 26
Structural and molecular determinants of Candida glabrata metacaspase maturation and activation by calcium. Commun Biol 5(1):1158 (2022)
Conchou L, Doumèche B, Galisson F, Violot S, Dugelay C, Diesis E, Page A, Bienvenu AL, Picot S, Aghajari N, Ballut L
RgGuinier 1.9 nm
Dmax 5.4 nm
VolumePorod 43 nm3

SASDQP5 – Phosphoprotein of Borna disease virus

Phosphoprotein experimental SAS data
Phosphoprotein of Borna disease virus Rg histogram
Sample: Phosphoprotein tetramer, 90 kDa Borna disease virus … protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5 mM β- mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Sep 1
Borna Disease Virus 1 Phosphoprotein Forms a Tetramer and Interacts with Host Factors Involved in DNA Double-Strand Break Repair and mRNA Processing. Viruses 14(11) (2022)
Tarbouriech N, Chenavier F, Kawasaki J, Bachiri K, Bourhis JM, Legrand P, Freslon LL, Laurent EMN, Suberbielle E, Ruigrok RWH, Tomonaga K, Gonzalez-Dunia D, Horie M, Coyaud E, Crépin T
RgGuinier 6.1 nm
Dmax 21.5 nm
VolumePorod 225 nm3

SASDQQ5 – Oligomerisation domain of phosphoprotein from Borna disease virus

Phosphoprotein experimental SAS data
DAMMIF model
Sample: Phosphoprotein tetramer, 47 kDa Borna disease virus … protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5 mM β- mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Sep 1
Borna Disease Virus 1 Phosphoprotein Forms a Tetramer and Interacts with Host Factors Involved in DNA Double-Strand Break Repair and mRNA Processing. Viruses 14(11) (2022)
Tarbouriech N, Chenavier F, Kawasaki J, Bachiri K, Bourhis JM, Legrand P, Freslon LL, Laurent EMN, Suberbielle E, Ruigrok RWH, Tomonaga K, Gonzalez-Dunia D, Horie M, Coyaud E, Crépin T
RgGuinier 4.5 nm
Dmax 17.0 nm
VolumePorod 66 nm3

SASDQR5 – Oligomerisation domain of phosphoprotein from Munia bornavirus

Phosphoprotein oligomerisation domain experimental SAS data
DAMMIF model
Sample: Phosphoprotein oligomerisation domain tetramer, 50 kDa protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5 mM β- mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Sep 1
Borna Disease Virus 1 Phosphoprotein Forms a Tetramer and Interacts with Host Factors Involved in DNA Double-Strand Break Repair and mRNA Processing. Viruses 14(11) (2022)
Tarbouriech N, Chenavier F, Kawasaki J, Bachiri K, Bourhis JM, Legrand P, Freslon LL, Laurent EMN, Suberbielle E, Ruigrok RWH, Tomonaga K, Gonzalez-Dunia D, Horie M, Coyaud E, Crépin T
RgGuinier 4.6 nm
Dmax 17.8 nm
VolumePorod 70 nm3

SASDQS5 – Oligomerisation domain of phosphoprotein from Gaboon viper virus

Phosphoprotein experimental SAS data
DAMMIF model
Sample: Phosphoprotein tetramer, 52 kDa Gaboon viper virus … protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5 mM β- mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Sep 1
Borna Disease Virus 1 Phosphoprotein Forms a Tetramer and Interacts with Host Factors Involved in DNA Double-Strand Break Repair and mRNA Processing. Viruses 14(11) (2022)
Tarbouriech N, Chenavier F, Kawasaki J, Bachiri K, Bourhis JM, Legrand P, Freslon LL, Laurent EMN, Suberbielle E, Ruigrok RWH, Tomonaga K, Gonzalez-Dunia D, Horie M, Coyaud E, Crépin T
RgGuinier 4.6 nm
Dmax 17.5 nm
VolumePorod 75 nm3