Browse by ORGANISM: other species

SASDW94 – Horse apoferritin from AF4-SAXS measurements

Ferritin light chain experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Ferritin light chain 24-mer, 480 kDa Equus caballus protein
Buffer: phosphate buffered saline, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Jun 19
AF4-to-SAXS: expanded characterization of nanoparticles and proteins at the P12 BioSAXS beamline. J Synchrotron Radiat (2025)
Da Vela S, Bartels K, Franke D, Soloviov D, Gräwert T, Molodenskiy D, Kolb B, Wilhelmy C, Drexel R, Meier F, Haas H, Langguth P, Graewert MA
RgGuinier 5.4 nm
Dmax 13.3 nm
VolumePorod 632 nm3

SASDWB4 – Sweet potato beta-amylase from AF4-SAXS measurement

Beta-amylase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Beta-amylase tetramer, 224 kDa Ipomoea batatas protein
Buffer: phosphate buffered saline, 1% glycerol, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Apr 13
AF4-to-SAXS: expanded characterization of nanoparticles and proteins at the P12 BioSAXS beamline. J Synchrotron Radiat (2025)
Da Vela S, Bartels K, Franke D, Soloviov D, Gräwert T, Molodenskiy D, Kolb B, Wilhelmy C, Drexel R, Meier F, Haas H, Langguth P, Graewert MA
RgGuinier 4.2 nm
Dmax 12.6 nm
VolumePorod 297 nm3

SASDRX6 – lantibiotic dehydratase MadB (apo)

Thiopeptide-type bacteriocin biosynthesis domain containing protein experimental SAS data
GASBOR model
Sample: Thiopeptide-type bacteriocin biosynthesis domain containing protein dimer, 250 kDa Clostridium sp. Maddingley … protein
Buffer: 50 mM HEPES, 200 mM NaCl, 1 % (v/v) Glycerol, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Jun 26
Structure of the lantibiotic dehydratase MadB
Jens Reiners
RgGuinier 4.5 nm
Dmax 13.6 nm
VolumePorod 440 nm3

SASDRY6 – lantibiotic dehydratase MadB bound to truncated maddinglicin with a full leader peptide (Leader3)

Thiopeptide-type bacteriocin biosynthesis domain containing proteinLantibiotic, gallidermin/nisin family experimental SAS data
GASBOR model
Sample: Thiopeptide-type bacteriocin biosynthesis domain containing protein dimer, 250 kDa Clostridium sp. Maddingley … protein
Lantibiotic, gallidermin/nisin family monomer, 3 kDa Clostridium sp. Maddingley … protein
Buffer: 50 mM HEPES, 200 mM NaCl, 1 % (v/v) Glycerol, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2020 Dec 3
Structure of the lantibiotic dehydratase MadB
Jens Reiners
RgGuinier 4.5 nm
Dmax 13.8 nm
VolumePorod 445 nm3

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

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