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SASDXD6 – Ubiquitin C-terminal hydrolase (UCH) domain of BAP1

Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 wild type experimental SAS data
Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 wild type Kratky plot
Sample: Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 wild type monomer, 27 kDa protein
Buffer: 20 mM HEPES, 150 mM NaCl, 3 mM CaCl2, 0.02% NaN3, pH: 7.5
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2024 Jun 23
Allosteric network of dynamic coupling within BAP1-UCH revealed by methyl NMR. Nat Commun (2026)
Lai CH, Lou YC, Chang CF, Lu WL, Sriramoju MK, Wang YS, Wu KP, Camilloni C, Hsu SD
RgGuinier 2.1 nm
Dmax 8.0 nm
VolumePorod 35 nm3

SASDXE6 – Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 point mutation (L49V)

Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 L49V experimental SAS data
Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 L49V Kratky plot
Sample: Ubiquitin C-terminal hydrolase (UCH) domain of BAP1 L49V monomer, 27 kDa protein
Buffer: 20 mM HEPES, 150 mM NaCl, 1 mM TCEP, 0.02% NaN3, pH: 7.5
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2024 Jun 23
Allosteric network of dynamic coupling within BAP1-UCH revealed by methyl NMR. Nat Commun (2026)
Lai CH, Lou YC, Chang CF, Lu WL, Sriramoju MK, Wang YS, Wu KP, Camilloni C, Hsu SD
RgGuinier 2.2 nm
Dmax 8.7 nm
VolumePorod 36 nm3

SASDVY7 – Glutamine C‐methyltransferase without cobalamin from Methanoculleus thermophilus

B12-binding domain/radical SAM domain protein, MJ_0865 family experimental SAS data
ALPHAFOLD model
Sample: B12-binding domain/radical SAM domain protein, MJ_0865 family monomer, 50 kDa Methanoculleus thermophilus protein
Buffer: 50 mM Tris, 300 mM NaCl, 5% glycerol, pH: 8
Experiment: SAXS data collected at SWING, SOLEIL on 2024 Sep 18
Insights into the stereochemical mechanism of the B(12)-dependent radical SAM glutamine C- methyltransferase (QCMT). Commun Biol (2026)
Bourdin T, Guillot A, Mauger M, Lefranc B, Gervason S, Glousieau M, Grimaldi S, Leprince J, Thureau A, Benjdia A, Berteau O
RgGuinier 2.6 nm
Dmax 10.4 nm
VolumePorod 85 nm3

SASDVZ7 – Glutamine C‐methyltransferase with cobalamin from Methanoculleus thermophilus

B12-binding domain/radical SAM domain protein, MJ_0865 family experimental SAS data
ALPHAFOLD model
Sample: B12-binding domain/radical SAM domain protein, MJ_0865 family monomer, 50 kDa Methanoculleus thermophilus protein
Buffer: 50 mM Tris, 300 mM NaCl, 5% glycerol, pH: 8
Experiment: SAXS data collected at SWING, SOLEIL on 2024 Sep 18
Insights into the stereochemical mechanism of the B(12)-dependent radical SAM glutamine C- methyltransferase (QCMT). Commun Biol (2026)
Bourdin T, Guillot A, Mauger M, Lefranc B, Gervason S, Glousieau M, Grimaldi S, Leprince J, Thureau A, Benjdia A, Berteau O
RgGuinier 2.5 nm
Dmax 10.1 nm
VolumePorod 78 nm3

SASDYW2 – IgA1 dimer - Control

Human immunoglobulin IgA1 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Human immunoglobulin IgA1 dimer, 320 kDa protein
Buffer: 8.2 mM Na2HPO4, 1.5 mM KH2PO4, 137 mM NaCl, 2.6 mM KCl (PBS), pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 7
Atomistic scattering modelling of the solution structure of human dimeric IgA1 reveals a structural and mechanistic basis for IgA nephropathy. J Biol Chem :113156 (2026)
Bhatt JS, Yeo SC, Ireland SM, Ben-Younis A, Gor J, Molyneux K, Barratt J, Perkins SJ
RgGuinier 8.7 nm
Dmax 35.0 nm

SASDYX2 – IgA1 dimer - Patient A

Human immunoglobulin IgA1 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Human immunoglobulin IgA1 dimer, 320 kDa protein
Buffer: PBS buffer, 137 mM NaCl, 8.2 mM Na2HPO4, 2.6 mM KCl, 1.5 mM KH2PO4, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 7
Atomistic scattering modelling of the solution structure of human dimeric IgA1 reveals a structural and mechanistic basis for IgA nephropathy. J Biol Chem :113156 (2026)
Bhatt JS, Yeo SC, Ireland SM, Ben-Younis A, Gor J, Molyneux K, Barratt J, Perkins SJ
RgGuinier 8.6 nm
Dmax 35.0 nm

SASDYY2 – IgA1 dimer - Patient B

Human immunoglobulin IgA1 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Human immunoglobulin IgA1 dimer, 320 kDa protein
Buffer: PBS buffer, 137 mM NaCl, 8.2 mM Na2HPO4, 2.6 mM KCl, 1.5 mM KH2PO4, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 7
Atomistic scattering modelling of the solution structure of human dimeric IgA1 reveals a structural and mechanistic basis for IgA nephropathy. J Biol Chem :113156 (2026)
Bhatt JS, Yeo SC, Ireland SM, Ben-Younis A, Gor J, Molyneux K, Barratt J, Perkins SJ
RgGuinier 8.4 nm
Dmax 35.0 nm

SASDYZ2 – IgA1 dimer - Patient C

Human immunoglobulin IgA1 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Human immunoglobulin IgA1 dimer, 320 kDa protein
Buffer: PBS buffer, 137 mM NaCl, 8.2 mM Na2HPO4, 2.6 mM KCl, 1.5 mM KH2PO4, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 7
Atomistic scattering modelling of the solution structure of human dimeric IgA1 reveals a structural and mechanistic basis for IgA nephropathy. J Biol Chem :113156 (2026)
Bhatt JS, Yeo SC, Ireland SM, Ben-Younis A, Gor J, Molyneux K, Barratt J, Perkins SJ
RgGuinier 8.5 nm
Dmax 35.0 nm

SASDUM8 – Collagenase G at pCa 3

Collagenase ColG (E656D, N659T, G836V, D837Y) experimental SAS data
MULTIFOXS model
Sample: Collagenase ColG (E656D, N659T, G836V, D837Y) monomer, 114 kDa Hathewaya histolytica protein
Buffer: 10 mM HEPES, 100 mM NaCl, 1 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2022 Oct 28
Collagenase G
Cody Brazel
RgGuinier 4.7 nm
Dmax 18.0 nm
VolumePorod 181 nm3

SASDUN8 – Collagenase G at pCa 4

Collagenase ColG (E656D, N659T, G836V, D837Y) experimental SAS data
MULTIFOXS model
Sample: Collagenase ColG (E656D, N659T, G836V, D837Y) monomer, 114 kDa Hathewaya histolytica protein
Buffer: 10 mM HEPES, 100 mM NaCl, 1 mM CaCl2, EDTA, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2022 Oct 28
Collagenase G
Cody Brazel
RgGuinier 4.7 nm
Dmax 19.0 nm
VolumePorod 182 nm3