|
|
|
|
|
| Sample: |
Double-stranded RNA-binding protein Staufen homolog 1 (Δ1-81) dimer, 110 kDa Homo sapiens protein
|
| Buffer: |
50 mM TRIS, 300 mM NaCl, 3.8 mM β-mercaptoethanol, pH: 7 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2021 Apr 23
|
Staufen-swapping motif is crucial for Staufen dimerization, structure, and Staufen-mediated mRNA decay.
Protein Sci 35(7):e70669 (2026)
Tripepi A, Shakoor H, Zlobina M, Klumpler T, Kubíčková M, Houser J, Klapetek P, Lukavsky PJ
|
| RgGuinier |
5.0 |
nm |
| Dmax |
14.1 |
nm |
| VolumePorod |
86 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Double-stranded RNA-binding protein Staufen homolog 1 (82-577), 55 kDa Homo sapiens protein
|
| Buffer: |
50 mM Tris-HCl, 300 mM NaCl, 3.6 mM β-mercaptoethanol, pH: 7 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2021 Apr 23
|
Staufen-swapping motif is crucial for Staufen dimerization, structure, and Staufen-mediated mRNA decay.
Protein Sci 35(7):e70669 (2026)
Tripepi A, Shakoor H, Zlobina M, Klumpler T, Kubíčková M, Houser J, Klapetek P, Lukavsky PJ
|
| RgGuinier |
5.0 |
nm |
| Dmax |
15.1 |
nm |
| VolumePorod |
92 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Double-stranded RNA-binding protein Staufen homolog 1 (81-577 + Δ454-488), 52 kDa Homo sapiens protein
|
| Buffer: |
50 mM Tris-HCl, 300 mM NaCl, 3.6 mM β-mercaptoethanol, pH: 7 |
| Experiment: |
SAXS
data collected at Rigaku BioSAXS-1000, CEITEC on 2020 Apr 5
|
Staufen-swapping motif is crucial for Staufen dimerization, structure, and Staufen-mediated mRNA decay.
Protein Sci 35(7):e70669 (2026)
Tripepi A, Shakoor H, Zlobina M, Klumpler T, Kubíčková M, Houser J, Klapetek P, Lukavsky PJ
|
| RgGuinier |
5.1 |
nm |
| Dmax |
13.8 |
nm |
| VolumePorod |
105 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Double-stranded RNA-binding protein Staufen homolog 1 (286-577), 32 kDa Homo sapiens protein
|
| Buffer: |
50 mM Tris-HCl, 150 mM NaCl, 3.6 mM β-mercaptoethanol, pH: 8 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2021 Apr 23
|
Staufen-swapping motif is crucial for Staufen dimerization, structure, and Staufen-mediated mRNA decay.
Protein Sci 35(7):e70669 (2026)
Tripepi A, Shakoor H, Zlobina M, Klumpler T, Kubíčková M, Houser J, Klapetek P, Lukavsky PJ
|
| RgGuinier |
4.0 |
nm |
| Dmax |
12.9 |
nm |
| VolumePorod |
46 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Double-stranded RNA-binding protein Staufen homolog 1 (286-577 + Δ454-488) monomer, 29 kDa Homo sapiens protein
|
| Buffer: |
50 mM Tris-HCl, 150 mM NaCl, 3.6 mM β-mercaptoethanol, pH: 8 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2020 Dec 17
|
Staufen-swapping motif is crucial for Staufen dimerization, structure, and Staufen-mediated mRNA decay.
Protein Sci 35(7):e70669 (2026)
Tripepi A, Shakoor H, Zlobina M, Klumpler T, Kubíčková M, Houser J, Klapetek P, Lukavsky PJ
|
| RgGuinier |
4.1 |
nm |
| Dmax |
19.5 |
nm |
| VolumePorod |
64 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Double-stranded RNA-binding protein Staufen homolog 1 (178-577), 44 kDa Homo sapiens protein
|
| Buffer: |
50 mM Tris-HCl, 150 mM NaCl, 3.6 mM β-mercaptoethanol, pH: 8 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2021 Apr 23
|
Staufen-swapping motif is crucial for Staufen dimerization, structure, and Staufen-mediated mRNA decay.
Protein Sci 35(7):e70669 (2026)
Tripepi A, Shakoor H, Zlobina M, Klumpler T, Kubíčková M, Houser J, Klapetek P, Lukavsky PJ
|
| RgGuinier |
4.6 |
nm |
| Dmax |
13.7 |
nm |
| VolumePorod |
89 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Double-stranded RNA-binding protein Staufen homolog 1 (178-577 + Δ454-488) monomer, 41 kDa Homo sapiens protein
|
| Buffer: |
50 mM Tris-HCl, 150 mM NaCl, 3.6 mM β-mercaptoethanol, pH: 8 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2020 Dec 17
|
Staufen-swapping motif is crucial for Staufen dimerization, structure, and Staufen-mediated mRNA decay.
Protein Sci 35(7):e70669 (2026)
Tripepi A, Shakoor H, Zlobina M, Klumpler T, Kubíčková M, Houser J, Klapetek P, Lukavsky PJ
|
| RgGuinier |
4.6 |
nm |
| Dmax |
16.9 |
nm |
| VolumePorod |
99 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Lipase chaperone monomer, 38 kDa Pseudomonas aeruginosa (strain … protein
|
| Buffer: |
50 mM Tris, 100 mM NaCl, 100 µM TCEP, 5% glycerol,, pH: 8 |
| Experiment: |
SAXS
data collected at Xenocs Xeuss 2.0 Q-Xoom, Center for Structural Studies, Heinrich-Heine-University on 2019 Nov 18
|
Conformational dynamics of the membrane-anchored foldase LipH from Pseudomonas aeruginosa facilitates recognition and release of the client lipase
Jens Reiners
|
| RgGuinier |
3.2 |
nm |
| Dmax |
12.6 |
nm |
| VolumePorod |
70 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
MosGCTL-3 dimer, 36 kDa Aedes aegypti protein
|
| Buffer: |
20 mM Tris, 250 mM NaCl, 2.5 mM CaCl2, pH: 7.5 |
| Experiment: |
SAXS
data collected at B21, Diamond Light Source on 2020 Dec 17
|
Conserved dimerization architecture in C-type lectins from virus-vector mosquitoes
Max Renner
|
|
|
|
|
|
|
|
| Sample: |
C-type lectin mosGCTL-1 dimer, 35 kDa Aedes aegypti protein
|
| Buffer: |
25 mM Citrate, 1 M NaCl, 10 mM CaCl2, pH: 4 |
| Experiment: |
SAXS
data collected at B21, Diamond Light Source on 2017 Aug 7
|
Conserved dimerization architecture in C-type lectins from virus-vector mosquitoes
Max Renner
|
|
|