Browse by ORGANISM: Homo sapiens (Human)

SASDNR3 – Fibrillin-1 fragment PF3

Fibrillin-1 PF3 experimental SAS data
DAMMIF model
Sample: Fibrillin-1 PF3 monomer, 78 kDa Homo sapiens protein
Buffer: Tris buffered saline, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2016 Dec 12
Latent TGFβ complexes are transglutaminase cross-linked to fibrillin to facilitate TGFβ activation. Matrix Biol (2022)
Lockhart-Cairns MP, Cain SA, Dajani R, Steer R, Thomson J, Alanazi YF, Kielty CM, Baldock C
RgGuinier 5.4 nm
Dmax 24.0 nm
VolumePorod 141 nm3

SASDNS3 – Latent-transforming growth factor beta-binding protein 1 C-terminus

Latent-transforming growth factor beta-binding protein 1 experimental SAS data
DAMMIF model
Sample: Latent-transforming growth factor beta-binding protein 1 monomer, 44 kDa Homo sapiens protein
Buffer: Tris buffered saline, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2016 Dec 12
Latent TGFβ complexes are transglutaminase cross-linked to fibrillin to facilitate TGFβ activation. Matrix Biol (2022)
Lockhart-Cairns MP, Cain SA, Dajani R, Steer R, Thomson J, Alanazi YF, Kielty CM, Baldock C
RgGuinier 4.7 nm
Dmax 20.5 nm
VolumePorod 102 nm3

SASDNT3 – Fibrillin-1 fragment PF3 crosslinked to latent transforming growth factor-beta-binding protein 1 C-terminus by transglutaminase 2

Latent-transforming growth factor beta-binding protein 1Fibrillin-1 PF3 experimental SAS data
DAMMIF model
Sample: Latent-transforming growth factor beta-binding protein 1 monomer, 44 kDa Homo sapiens protein
Fibrillin-1 PF3 monomer, 78 kDa Homo sapiens protein
Buffer: 10 mM Hepes, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2017 Jul 20
Latent TGFβ complexes are transglutaminase cross-linked to fibrillin to facilitate TGFβ activation. Matrix Biol (2022)
Lockhart-Cairns MP, Cain SA, Dajani R, Steer R, Thomson J, Alanazi YF, Kielty CM, Baldock C
RgGuinier 7.4 nm
Dmax 29.6 nm
VolumePorod 759 nm3

SASDKS4 – Teneurin-4 dimer wildtype in SEC buffer (20 mM HEPES, 150 mM NaCl)

Teneurin-4 experimental SAS data
Teneurin-4 dimer wildtype in SEC buffer (20 mM HEPES, 150 mM NaCl) Rg histogram
Sample: Teneurin-4 dimer, 537 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.8
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 16
Teneurin4 dimer structures reveal a calcium‐stabilized compact conformation supporting homomeric trans‐interactions The EMBO Journal (2022)
Meijer D, Frias C, Beugelink J, Deurloo Y, Janssen B
RgGuinier 7.8 nm
Dmax 32.0 nm
VolumePorod 1280 nm3

SASDKT4 – Teneurin-4 dimer wildtype in SEC buffer with calcium (20 mM HEPES, 150 mM NaCl, 2 mM CaCl2)

Teneurin-4 experimental SAS data
Teneurin-4 dimer wildtype in SEC buffer with calcium (20 mM HEPES, 150 mM NaCl, 2 mM CaCl2) Rg histogram
Sample: Teneurin-4 dimer, 537 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2 mM CaCl2, pH: 7.8
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 16
Teneurin4 dimer structures reveal a calcium‐stabilized compact conformation supporting homomeric trans‐interactions The EMBO Journal (2022)
Meijer D, Frias C, Beugelink J, Deurloo Y, Janssen B
RgGuinier 7.2 nm
Dmax 29.5 nm
VolumePorod 1270 nm3

SASDKU4 – Teneurin-4 dimer wildtype in SEC buffer with EDTA (20 mM HEPES, 150 mM NaCl, 2 mM EDTA)

Teneurin-4 experimental SAS data
Teneurin-4 dimer wildtype in SEC buffer with EDTA (20 mM HEPES, 150 mM NaCl, 2 mM EDTA) Rg histogram
Sample: Teneurin-4 dimer, 537 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2 mM EDTA, pH: 7.8
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 16
Teneurin4 dimer structures reveal a calcium‐stabilized compact conformation supporting homomeric trans‐interactions The EMBO Journal (2022)
Meijer D, Frias C, Beugelink J, Deurloo Y, Janssen B
RgGuinier 9.5 nm
Dmax 40.0 nm
VolumePorod 1370 nm3

SASDKV4 – Teneurin-4 dimer mutant in SEC buffer (20 mM HEPES, 150 mM NaCl)

Teneurin-4 (S2585C) experimental SAS data
Teneurin-4 dimer mutant in SEC buffer (20 mM HEPES, 150 mM NaCl) Rg histogram
Sample: Teneurin-4 (S2585C) dimer, 537 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.8
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 16
Teneurin4 dimer structures reveal a calcium‐stabilized compact conformation supporting homomeric trans‐interactions The EMBO Journal (2022)
Meijer D, Frias C, Beugelink J, Deurloo Y, Janssen B
RgGuinier 7.1 nm
Dmax 29.5 nm
VolumePorod 1260 nm3

SASDKW4 – Teneurin-4 dimer mutant in SEC buffer with calcium (20 mM HEPES, 150 mM NaCl, 2 mM CaCl2)

Teneurin-4 (S2585C) experimental SAS data
Teneurin-4 dimer mutant in SEC buffer with calcium (20 mM HEPES, 150 mM NaCl, 2 mM CaCl2) Rg histogram
Sample: Teneurin-4 (S2585C) dimer, 537 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2 mM CaCl2, pH: 7.8
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 16
Teneurin4 dimer structures reveal a calcium‐stabilized compact conformation supporting homomeric trans‐interactions The EMBO Journal (2022)
Meijer D, Frias C, Beugelink J, Deurloo Y, Janssen B
RgGuinier 7.0 nm
Dmax 29.5 nm
VolumePorod 1270 nm3

SASDKX4 – Teneurin-4 dimer mutant in SEC buffer with EDTA (20 mM HEPES, 150 mM NaCl, 2 mM EDTA)

Teneurin-4 (S2585C) experimental SAS data
Teneurin-4 dimer mutant in SEC buffer with EDTA (20 mM HEPES, 150 mM NaCl, 2 mM EDTA) Rg histogram
Sample: Teneurin-4 (S2585C) dimer, 537 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2 mM EDTA, pH: 7.8
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 16
Teneurin4 dimer structures reveal a calcium‐stabilized compact conformation supporting homomeric trans‐interactions The EMBO Journal (2022)
Meijer D, Frias C, Beugelink J, Deurloo Y, Janssen B
RgGuinier 7.8 nm
Dmax 31.0 nm
VolumePorod 1390 nm3

SASDMY7 – Poly-histidine tagged Myosin X component at 8979 eV

Unconventional myosin-X component experimental SAS data
Unconventional myosin-X component Kratky plot
Sample: Unconventional myosin-X component dimer, 15 kDa Homo sapiens protein
Buffer: HEPES, 5% glycerol, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BL-15A2, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2021 Mar 16
K -edge anomalous SAXS for protein solution structure modeling Acta Crystallographica Section D Structural Biology 78(2) (2022)
Virk K, Yonezawa K, Choukate K, Singh L, Shimizu N, Chaudhuri B
RgGuinier 2.2 nm
Dmax 8.5 nm
VolumePorod 24 nm3