|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
Sample: |
Procollagen galactosyltransferase 1 dimer, 137 kDa Homo sapiens protein
|
Buffer: |
25 mM HEPES, 0.1 M NaCl, pH: 8
|
Experiment: |
SAXS
data collected at BM29, ESRF on 2022 Jun 5
|
Molecular Characterization of Human Collagen Hydroxylysine Galactosyltransferase GLT25D1/COLGALT1
Federico Forneris
|
RgGuinier |
4.3 |
nm |
Dmax |
14.0 |
nm |
VolumePorod |
184 |
nm3 |
|
|
|
|
|
Sample: |
humanized immunoglobulin G4 monoclonal antibody (lebrikizumab) monomer, 148 kDa Mouse/human protein
|
Buffer: |
100 mM glycine-HCl, 200 mM NaCl, pH: 2
|
Experiment: |
SAXS
data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2024 Nov 19
|
IgG4
and IgG1
undergo common acid‐induced compaction into an alternatively folded state
FEBS Letters (2025)
Imamura H, Honda S
|
RgGuinier |
4.1 |
nm |
Dmax |
14.0 |
nm |
VolumePorod |
238 |
nm3 |
|
|
|
|
|
Sample: |
humanized immunoglobulin G1 monoclonal antibody (trastuzumab) monomer, 148 kDa Mouse/human protein
|
Buffer: |
100 mM glycine-HCl, 200 mM NaCl, pH: 2
|
Experiment: |
SAXS
data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2023 May 20
|
IgG4
and IgG1
undergo common acid‐induced compaction into an alternatively folded state
FEBS Letters (2025)
Imamura H, Honda S
|
RgGuinier |
4.2 |
nm |
Dmax |
12.9 |
nm |
VolumePorod |
240 |
nm3 |
|
|
|
|
|
Sample: |
humanized immunoglobulin G4 monoclonal antibody (lebrikizumab) monomer, 148 kDa Mouse/human protein
|
Buffer: |
10 mM sodium phosphate, pH: 7
|
Experiment: |
SAXS
data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2024 Nov 19
|
IgG4
and IgG1
undergo common acid‐induced compaction into an alternatively folded state
FEBS Letters (2025)
Imamura H, Honda S
|
RgGuinier |
4.8 |
nm |
Dmax |
15.6 |
nm |
VolumePorod |
211 |
nm3 |
|
|
|
|
|
Sample: |
Alpha-1-acid glycoprotein 1 monomer, 22 kDa Homo sapiens protein
|
Buffer: |
phosphate buffered saline, pH: 7.4
|
Experiment: |
SAXS
data collected at Anton Paar SAXSpace, CSIR - Institute of Microbial Technology (IMTech) on 2021 Jan 12
|
SAXS data based glycosylated models of human alpha-1-acid glycorprotein, a key player in health, disease and drug circulation.
J Biomol Struct Dyn :1-15 (2025)
Kalidas N, Peddada N, Pandey K, Ashish
|
RgGuinier |
2.6 |
nm |
Dmax |
7.5 |
nm |
VolumePorod |
83 |
nm3 |
|
|
|
|
|
Sample: |
Alpha-1-acid glycoprotein 1 monomer, 22 kDa Homo sapiens protein
|
Buffer: |
phosphate buffered saline, pH: 7.4
|
Experiment: |
SAXS
data collected at Anton Paar SAXSpace, CSIR - Institute of Microbial Technology (IMTech) on 2021 Jan 12
|
SAXS data based glycosylated models of human alpha-1-acid glycorprotein, a key player in health, disease and drug circulation.
J Biomol Struct Dyn :1-15 (2025)
Kalidas N, Peddada N, Pandey K, Ashish
|
RgGuinier |
2.5 |
nm |
Dmax |
7.5 |
nm |
VolumePorod |
96 |
nm3 |
|
|
|
|
|
Sample: |
Auxin response factor monomer, 46 kDa Marchantia polymorpha protein
|
Buffer: |
20 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, pH: 8
|
Experiment: |
SAXS
data collected at BL11 - NCD, ALBA on 2019 Dec 3
|
The structure and function of the DNA binding domain of class B MpARF2 share more traits with class A AtARF5 than to that of class B AtARF1.
Structure (2025)
Crespo I, Malfois M, Rienstra J, Tarrés-Solé A, van den Berg W, Weijers D, Boer DR
|
RgGuinier |
2.6 |
nm |
Dmax |
6.2 |
nm |
VolumePorod |
59 |
nm3 |
|
|