Browse by MACROMOLECULE type: protein

SASDSQ6 – Human RAD23B, ∆UBA-1 domain deletion (RAD23B∆UBA1)

UV excision repair protein RAD23 homolog B (∆186-231) experimental SAS data
UV excision repair protein RAD23 homolog B (∆186-231) Kratky plot
Sample: UV excision repair protein RAD23 homolog B (∆186-231) monomer, 38 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 0.5 mM EDTA, 0.02 % NaN3, pH: 6.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Feb 22
Domain deletion constructs of hHR23B
Sarasi Galagedera
RgGuinier 4.6 nm
Dmax 21.7 nm
VolumePorod 95 nm3

SASDSR6 – Human RAD23B, ∆UBA-2 domain deletion (RAD23B∆UBA2)

UV excision repair protein RAD23 homolog B (∆362-409) experimental SAS data
UV excision repair protein RAD23 homolog B (∆362-409) Kratky plot
Sample: UV excision repair protein RAD23 homolog B (∆362-409) monomer, 38 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 0.5 mM EDTA, 0.02 % NaN3, pH: 6.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Feb 22
Domain deletion constructs of hHR23B
Sarasi Galagedera
RgGuinier 4.1 nm
Dmax 17.5 nm
VolumePorod 79 nm3

SASDSS6 – Human RAD23B, ∆STI1 domain deletion (RAD23B∆STI1)

UV excision repair protein RAD23 homolog B (∆274-306) experimental SAS data
UV excision repair protein RAD23 homolog B (∆274-306) Kratky plot
Sample: UV excision repair protein RAD23 homolog B (∆274-306) monomer, 39 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 0.5 mM EDTA, 0.02 % NaN3, pH: 6.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Feb 22
Domain deletion constructs of hHR23B
Sarasi Galagedera
RgGuinier 4.6 nm
Dmax 24.2 nm
VolumePorod 103 nm3

SASDST6 – Human RAD23B with ∆UBA-1 and ∆UBA-2 domain deletions (RAD23B∆UBA1∆UBA2)

UV excision repair protein RAD23 homolog B (∆186-231, ∆362-409) experimental SAS data
UV excision repair protein RAD23 homolog B (∆186-231, ∆362-409) Kratky plot
Sample: UV excision repair protein RAD23 homolog B (∆186-231, ∆362-409) monomer, 33 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 0.5 mM EDTA, 0.02 % NaN3, pH: 6.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Feb 22
Domain deletion constructs of hHR23B
Sarasi Galagedera
RgGuinier 4.9 nm
Dmax 25.5 nm
VolumePorod 100 nm3

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