SASDV98 – Full-length N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF

N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF experimental SAS data
Full-length N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF Rg histogram
Sample: N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF tetramer, 223 kDa Aspergillus fumigatus (strain … protein
Buffer: 50 mM Tris, 200 mM NaCl, 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 Jul 7
SidF, a dual substrate N5-acetyl-N5-hydroxy-L-ornithine transacetylase involved in Aspergillus fumigatus siderophore biosynthesis Journal of Structural Biology: X 11:100119 (2025)
Poonsiri T, Stransky J, Demitri N, Haas H, Cianci M, Benini S
RgGuinier 4.0 nm
Dmax 19.0 nm
VolumePorod 412 nm3

SASDVA8 – The N-terminal domain of N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF

N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF experimental SAS data
The N-terminal domain of N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF Rg histogram
Sample: N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF monomer, 25 kDa Aspergillus fumigatus (strain … protein
Buffer: 50 mM Tris, 200 mM NaCl, pH: 8
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2023 Jan 18
SidF, a dual substrate N5-acetyl-N5-hydroxy-L-ornithine transacetylase involved in Aspergillus fumigatus siderophore biosynthesis Journal of Structural Biology: X 11:100119 (2025)
Poonsiri T, Stransky J, Demitri N, Haas H, Cianci M, Benini S
RgGuinier 2.2 nm
Dmax 8.9 nm
VolumePorod 30 nm3

SASDVB8 – C-terminal truncation mutant of N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF

N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF (Δ444-462) experimental SAS data
CORAL model
Sample: N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF (Δ444-462) dimer, 107 kDa Aspergillus fumigatus (strain … protein
Buffer: 50 mM Tris, 200 mM NaCl, pH: 8
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2023 Jan 18
SidF, a dual substrate N5-acetyl-N5-hydroxy-L-ornithine transacetylase involved in Aspergillus fumigatus siderophore biosynthesis Journal of Structural Biology: X 11:100119 (2025)
Poonsiri T, Stransky J, Demitri N, Haas H, Cianci M, Benini S
RgGuinier 3.5 nm
Dmax 15.0 nm
VolumePorod 189 nm3

SASDVD6 – The Ig-like C2-type 4 domain (Ig4WT) of Palladin

Palladin experimental SAS data
SASREF model
Sample: Palladin monomer, 12 kDa Mus musculus protein
Buffer: 20 mM HEPES pH 7.4, 1 mM DTT, 100 mM NaCl, pH:
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2023 Aug 29
Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS. Protein Sci 34(5):e70122 (2025)
Sargent R, Liu DH, Yadav R, Glennenmeier D, Bradford C, Urbina N, Beck MR
RgGuinier 1.7 nm
Dmax 6.8 nm
VolumePorod 18 nm3

SASDVE6 – The Ig-like C2-type 3 domain (Ig3WT) of Palladin

Palladin experimental SAS data
SASREF model
Sample: Palladin monomer, 12 kDa Mus musculus protein
Buffer: 20 mM HEPES pH 7.4, 1 mM DTT, 100 mM NaCl, pH:
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2023 Aug 29
Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS. Protein Sci 34(5):e70122 (2025)
Sargent R, Liu DH, Yadav R, Glennenmeier D, Bradford C, Urbina N, Beck MR
RgGuinier 1.6 nm
Dmax 6.7 nm
VolumePorod 18 nm3

SASDVF6 – The Ig-like C2-type 3 and Ig-like C2-type 4 domains (Ig34WT) of Palladin

Palladin experimental SAS data
The Ig-like C2-type 3 and Ig-like C2-type 4 domains (Ig34WT) of Palladin Rg histogram
Sample: Palladin monomer, 27 kDa Mus musculus protein
Buffer: 20 mM HEPES pH 7.4, 1 mM DTT, 100 mM NaCl, pH:
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2023 Aug 29
Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS. Protein Sci 34(5):e70122 (2025)
Sargent R, Liu DH, Yadav R, Glennenmeier D, Bradford C, Urbina N, Beck MR
RgGuinier 2.8 nm
Dmax 12.3 nm
VolumePorod 29 nm3

SASDRK9 – single self-amplifying RNA

self-amplifying RNA experimental SAS data
DAMMIF model
Sample: self-amplifying RNA monomer, 3030 kDa RNA
Buffer: MBG buffer: 5% w/v D-Glucose, 10mM MES (2-(N-morpholino)ethanesulfonic acid) in double distillated sterile/RNAse free water, pH: 6.1
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Nov 10
Compact polyethylenimine-complexed mRNA molecules as quintessential vaccines
Martin Schroer
RgGuinier 90.5 nm
Dmax 200.0 nm

SASDRL9 – single self-amplifying RNA + 50 mM NaCl

self-amplifying RNA experimental SAS data
DAMMIF model
Sample: self-amplifying RNA monomer, 3030 kDa RNA
Buffer: MBG buffer: 5% w/v D-Glucose, 10mM MES (2-(N-morpholino)ethanesulfonic acid) in double distillated sterile/RNAse free water, pH: 6.1
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Mar 10
Compact polyethylenimine-complexed mRNA molecules as quintessential vaccines
Martin Schroer
RgGuinier 30.7 nm
Dmax 107.4 nm
VolumePorod 112000 nm3

SASDRM9 – Polyethylenimine-compacted single self-amplifying RNA for prophylactic and therapeutic application, specifically for vaccination

self-amplifying RNAlinear polyethylenimine experimental SAS data
DAMMIF model
Sample: self-amplifying RNA monomer, 3030 kDa RNA
linear polyethylenimine monomer, 25 kDa none (polymer)
Buffer: MBG buffer: 5% w/v D-Glucose, 10mM MES (2-(N-morpholino)ethanesulfonic acid) in double distillated sterile/RNAse free water, pH: 6.1
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Nov 10
Compact polyethylenimine-complexed mRNA molecules as quintessential vaccines
Martin Schroer
RgGuinier 12.0 nm
Dmax 40.0 nm
VolumePorod 9100 nm3

SASDV74 – Ser48-phosphorylated N-terminal domain of transactive response DNA-binding protein 43 (TDP-43)

TAR DNA-binding protein 43 experimental SAS data
DAMMIF model
Sample: TAR DNA-binding protein 43 monomer, 9 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, 3% glycerol,, pH: 8.5
Experiment: SAXS data collected at BL38B1, SPring-8 on 2024 May 29
Semi-synthesis of TDP-43 reveals the effects of phosphorylation in N-terminal domain on self-association Communications Chemistry 8(1) (2025)
Sasaki D, Tenda M, Sohma Y
RgGuinier 1.4 nm
Dmax 4.3 nm
VolumePorod 15 nm3

4690 hits found.