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SASDPP3 – RTX719. Double-acylated truncated variant of B. pertussis adenylate cyclase toxin (CyaA)

Double-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 experimental SAS data
RTX719. Double-acylated truncated variant of B. pertussis adenylate cyclase toxin (CyaA) Rg histogram
Sample: Double-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 monomer, 78 kDa Bordetella pertussis protein
Buffer: 50 mM NaCl, 3 mM CaCl2, 20 mM Tris, pH: 8
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Feb 15
Acyl chains stabilize the acylated domain and determine the receptor-mediated interaction of the Bordetella adenylate cyclase toxin with cell membrane. J Biol Chem :110392 (2025)
Espinosa-Vinals C, Stransky J, Osicka R, Osickova A, Jurnecka D, Sebo P, Bumba L
RgGuinier 3.4 nm
Dmax 14.5 nm
VolumePorod 67 nm3

SASDPQ3 – RTX719-K860R. Mono-acylated truncated variant of B. pertussis adenylate cyclase toxin (CyaA)

Mono-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 experimental SAS data
RTX719-K860R. Mono-acylated truncated variant of B. pertussis adenylate cyclase toxin (CyaA) Rg histogram
Sample: Mono-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 monomer, 78 kDa Bordetella pertussis protein
Buffer: 50 mM NaCl, 3 mM CaCl2, 20 mM Tris, pH: 8
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Feb 16
Acyl chains stabilize the acylated domain and determine the receptor-mediated interaction of the Bordetella adenylate cyclase toxin with cell membrane. J Biol Chem :110392 (2025)
Espinosa-Vinals C, Stransky J, Osicka R, Osickova A, Jurnecka D, Sebo P, Bumba L
RgGuinier 5.0 nm
Dmax 25.8 nm
VolumePorod 178 nm3

SASDPR3 – RTX719-K983R. Mono-acylated truncated variant of B. pertussis adenylate cyclase toxin (CyaA)

Mono-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 experimental SAS data
RTX719-K983R. Mono-acylated truncated variant of B. pertussis adenylate cyclase toxin (CyaA) Rg histogram
Sample: Mono-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 monomer, 78 kDa Bordetella pertussis protein
Buffer: 50 mM NaCl, 3 mM CaCl2, 20 mM Tris, pH: 8
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Feb 17
Acyl chains stabilize the acylated domain and determine the receptor-mediated interaction of the Bordetella adenylate cyclase toxin with cell membrane. J Biol Chem :110392 (2025)
Espinosa-Vinals C, Stransky J, Osicka R, Osickova A, Jurnecka D, Sebo P, Bumba L
RgGuinier 5.3 nm
Dmax 26.3 nm
VolumePorod 187 nm3

SASDPS3 – proRTX719. Non-acylated truncated variant of B. pertussis adenylate cyclase toxin (CyaA)

Non-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 experimental SAS data
proRTX719. Non-acylated truncated variant of B. pertussis adenylate cyclase toxin (CyaA) Rg histogram
Sample: Non-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 monomer, 78 kDa Bordetella pertussis protein
Buffer: 50 mM NaCl, 3 mM CaCl2, 20 mM Tris, pH: 8
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Feb 22
Acyl chains stabilize the acylated domain and determine the receptor-mediated interaction of the Bordetella adenylate cyclase toxin with cell membrane. J Biol Chem :110392 (2025)
Espinosa-Vinals C, Stransky J, Osicka R, Osickova A, Jurnecka D, Sebo P, Bumba L
RgGuinier 4.2 nm
Dmax 17.8 nm
VolumePorod 133 nm3

SASDVE7 – Hexameric L-threonine dehydratase biosynthetic (IlvA) from Staphylococcus aureus

L-threonine dehydratase biosynthetic IlvA experimental SAS data
CHIMERA model
Sample: L-threonine dehydratase biosynthetic IlvA hexamer, 288 kDa Staphylococcus aureus (strain … protein
Buffer: 20 mM KPO4, 200 mM NaCl, 0.1 mM TCEP,, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Oct 14
Isoleucine Binding and Regulation of Escherichia coli and Staphylococcus aureus Threonine Dehydratase (IlvA). Biochemistry (2025)
Yun MK, Subramanian C, Miller K, Jackson P, Radka CD, Rock CO
RgGuinier 5.1 nm
Dmax 17.1 nm
VolumePorod 386 nm3

SASDSR9 – SARS-CoV-2 N-protein (N1-245; residues 1-245): 38.2 µM

Nucleoprotein experimental SAS data
Nucleoprotein Kratky plot
Sample: Nucleoprotein monomer, 27 kDa Severe acute respiratory … protein
Buffer: 100 mM Tris-HCl, 150 mM NaCl, 1 mM EDTA, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 May 13
Dynamic ensembles of SARS-CoV-2 N-protein reveal head-to-head coiled-coil-driven oligomerization and phase separation. Nucleic Acids Res 53(11) (2025)
Hernandez G, Martins ML, Fernandes NP, Veloso T, Lopes J, Gomes T, Cordeiro TN
RgGuinier 3.3 nm
Dmax 15.5 nm
VolumePorod 56 nm3

SASDSS9 – SARS-CoV-2 N-protein (N1-245, residues 1-245): 76.4 µM

Nucleoprotein experimental SAS data
Nucleoprotein Kratky plot
Sample: Nucleoprotein dimer, 55 kDa Severe acute respiratory … protein
Buffer: 100 mM Tris-HCl, 150 mM NaCl, 1 mM EDTA, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 May 13
Dynamic ensembles of SARS-CoV-2 N-protein reveal head-to-head coiled-coil-driven oligomerization and phase separation. Nucleic Acids Res 53(11) (2025)
Hernandez G, Martins ML, Fernandes NP, Veloso T, Lopes J, Gomes T, Cordeiro TN
RgGuinier 4.0 nm
Dmax 18.0 nm
VolumePorod 67 nm3

SASDST9 – SARS-CoV-2 N-protein (N1-245; residues 1-245): 294.7 µM

Nucleoprotein experimental SAS data
Nucleoprotein Kratky plot
Sample: Nucleoprotein tetramer, 110 kDa Severe acute respiratory … protein
Buffer: 100 mM Tris-HCl, 150 mM NaCl, 1 mM EDTA, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 May 13
Dynamic ensembles of SARS-CoV-2 N-protein reveal head-to-head coiled-coil-driven oligomerization and phase separation. Nucleic Acids Res 53(11) (2025)
Hernandez G, Martins ML, Fernandes NP, Veloso T, Lopes J, Gomes T, Cordeiro TN
RgGuinier 5.2 nm
Dmax 22.0 nm
VolumePorod 117 nm3

SASDSU9 – SARS-CoV-2 N-protein (N1-245, residues 1-245): 400 µM

Nucleoprotein experimental SAS data
Nucleoprotein Kratky plot
Sample: Nucleoprotein tetramer, 110 kDa Severe acute respiratory … protein
Buffer: 100 mM Tris-HCl, 150 mM NaCl, 1 mM EDTA, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 May 13
Dynamic ensembles of SARS-CoV-2 N-protein reveal head-to-head coiled-coil-driven oligomerization and phase separation. Nucleic Acids Res 53(11) (2025)
Hernandez G, Martins ML, Fernandes NP, Veloso T, Lopes J, Gomes T, Cordeiro TN
RgGuinier 5.4 nm
Dmax 24.0 nm
VolumePorod 157 nm3

SASDSV9 – SARS-CoV-2 N-protein (N1-245; residues 1-245) L223P, L227P and L230P triple mutant: 36.4 µM

Nucleoprotein (L223P, L227P, L230P) experimental SAS data
Nucleoprotein (L223P, L227P, L230P) Kratky plot
Sample: Nucleoprotein (L223P, L227P, L230P) monomer, 27 kDa Severe acute respiratory … protein
Buffer: 100 mM Tris-HCl, 150 mM NaCl, 1 mM EDTA, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Jan 29
Dynamic ensembles of SARS-CoV-2 N-protein reveal head-to-head coiled-coil-driven oligomerization and phase separation. Nucleic Acids Res 53(11) (2025)
Hernandez G, Martins ML, Fernandes NP, Veloso T, Lopes J, Gomes T, Cordeiro TN
RgGuinier 3.2 nm
Dmax 13.5 nm
VolumePorod 53 nm3