Browse by ORGANISM: other species

SASDUD9 – Apical stem loop of stem loop 2 motif (s2m) in Delta variant of SARS-CoV-2

apical stem loop of stem loop 2 motif (s2m) in Delta variant of SARS-CoV-2 experimental SAS data
apical stem loop of stem loop 2 motif (s2m) in Delta variant of SARS-CoV-2 Kratky plot
Sample: Apical stem loop of stem loop 2 motif (s2m) in Delta variant of SARS-CoV-2 monomer, 8 kDa SARS-Coronavirus-2 Delta RNA
Buffer: 50 mM Bis-Tris, 25 mM NaCl, pH: 6.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2022 Nov 30
Structural heterogeneity and dynamics in the apical stem loop of s2m from SARS-CoV-2 Delta by an integrative NMR spectroscopy and MD simulation approach. Nucleic Acids Res 53(12) (2025)
Wirtz Martin MA, Makowski JA, Matzel T, Kensinger AH, Herr A, Richter C, Jonker HRA, Wacker A, Evanseck JD, Schwalbe H
RgGuinier 1.5 nm

SASDWL5 – I-RNA, an A-to-I hyper-edited 20mer dsRNA

I-RNA, Top-strandI-RNA, Bottom-strand experimental SAS data
I-RNA, Top-strand I-RNA, Bottom-strand Kratky plot
Sample: I-RNA, Top-strand monomer, 7 kDa RNA
I-RNA, Bottom-strand monomer, 7 kDa RNA
Buffer: 25 mM sodium phosphate 25 mM sodium chloride, pH: 6.4
Experiment: SAXS data collected at BM29, ESRF on 2022 Nov 9
Unique conformational dynamics and protein recognition of A-to-I hyper-edited dsRNA. Nucleic Acids Res 53(12) (2025)
Müller-Hermes C, Piomponi V, Hilber S, Asami S, Kreutz C, Bussi G, Sattler M
RgGuinier 2.0 nm
Dmax 6.9 nm
VolumePorod 17 nm3

SASDWM5 – A-RNA, non-edited 20mer dsRNA

A-RNA, Top-StrandA-RNA, Bottom-Strand experimental SAS data
A-RNA, Top-Strand A-RNA, Bottom-Strand Kratky plot
Sample: A-RNA, Top-Strand monomer, 6 kDa RNA
A-RNA, Bottom-Strand monomer, 6 kDa RNA
Buffer: 25 mM sodium phosphate 25 mM sodium chloride, pH: 6.4
Experiment: SAXS data collected at BM29, ESRF on 2022 Nov 9
Unique conformational dynamics and protein recognition of A-to-I hyper-edited dsRNA. Nucleic Acids Res 53(12) (2025)
Müller-Hermes C, Piomponi V, Hilber S, Asami S, Kreutz C, Bussi G, Sattler M
RgGuinier 1.8 nm
Dmax 6.2 nm
VolumePorod 17 nm3

SASDXB3 – Apical stem loop of stem loop 2 motif in Delta variant of SARS-CoV-2 (s2m Delta_short)

apical stem loop of stem loop 2 motif (s2m) in Delta variant of SARS-CoV-2 experimental SAS data
apical stem loop of stem loop 2 motif (s2m) in Delta variant of SARS-CoV-2 Kratky plot
Sample: Apical stem loop of stem loop 2 motif (s2m) in Delta variant of SARS-CoV-2 monomer, 8 kDa SARS-Coronavirus-2 Delta RNA
Buffer: 50 mM Bis-Tris, 25 mM NaCl, pH: 6.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2022 Nov 30
Structural heterogeneity and dynamics in the apical stem loop of s2m from SARS-CoV-2 Delta by an integrative NMR spectroscopy and MD simulation approach. Nucleic Acids Res 53(12) (2025)
Wirtz Martin MA, Makowski JA, Matzel T, Kensinger AH, Herr A, Richter C, Jonker HRA, Wacker A, Evanseck JD, Schwalbe H
RgGuinier 1.4 nm

SASDXK3 – Alkaline serine protease (36 kDa peptidase core domain, StmPr1)

Alkaline serine protease experimental SAS data
Alkaline serine protease Kratky plot
Sample: Alkaline serine protease monomer, 36 kDa Stenotrophomonas maltophilia protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Jun 10
Unveiling the structure, function and dynamics of StmPr1 in Stenotrophomonas maltophilia virulence. Sci Rep 15(1):20193 (2025)
Sommer M, Negm A, Outzen L, Windhorst S, Gabdulkhakov A, Weber W, Betzel C
RgGuinier 1.9 nm
Dmax 5.5 nm
VolumePorod 44 nm3

SASDXL3 – Alkaline serine protease (47 kDa peptidase core and C-terminal domains, StmPr1)

Alkaline serine protease (Δ1-150) experimental SAS data
Alkaline serine protease (Δ1-150) Kratky plot
Sample: Alkaline serine protease (Δ1-150) monomer, 47 kDa Stenotrophomonas maltophilia protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Nov 25
Unveiling the structure, function and dynamics of StmPr1 in Stenotrophomonas maltophilia virulence. Sci Rep 15(1):20193 (2025)
Sommer M, Negm A, Outzen L, Windhorst S, Gabdulkhakov A, Weber W, Betzel C
RgGuinier 2.9 nm
Dmax 10.0 nm
VolumePorod 112 nm3

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