Browse by MODEL: Hybrid

SASDLN3 – Interleukin 11 signalling complex, full-length extracellular gp130

Interleukin-11Interleukin-11 receptor subunit alphaInterleukin-6 receptor subunit beta experimental SAS data
OTHER model
Sample: Interleukin-11 dimer, 36 kDa Homo sapiens protein
Interleukin-11 receptor subunit alpha dimer, 64 kDa Homo sapiens protein
Interleukin-6 receptor subunit beta dimer, 134 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Nov 28
Structures of the interleukin 11 signalling complex reveal gp130 dynamics and the inhibitory mechanism of a cytokine variant Nature Communications 14(1) (2023)
Metcalfe R, Hanssen E, Fung K, Aizel K, Kosasih C, Zlatic C, Doughty L, Morton C, Leis A, Parker M, Gooley P, Putoczki T, Griffin M
RgGuinier 6.2 nm
Dmax 20.7 nm
VolumePorod 710 nm3

SASDLP3 – Interleukin 11 complex with IL-11Rα and gp130 D2-D3

Interleukin-11 receptor subunit alphaInterleukin 11Interleukin-6 receptor subunit beta experimental SAS data
OTHER model
Sample: Interleukin-11 receptor subunit alpha monomer, 32 kDa Homo sapiens protein
Interleukin 11 monomer, 18 kDa Homo sapiens protein
Interleukin-6 receptor subunit beta monomer, 23 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 8
Structures of the interleukin 11 signalling complex reveal gp130 dynamics and the inhibitory mechanism of a cytokine variant Nature Communications 14(1) (2023)
Metcalfe R, Hanssen E, Fung K, Aizel K, Kosasih C, Zlatic C, Doughty L, Morton C, Leis A, Parker M, Gooley P, Putoczki T, Griffin M
RgGuinier 3.6 nm
Dmax 12.9 nm
VolumePorod 127 nm3

SASDLQ3 – Interleukin 11, W168A mutant

Interleukin-11 (W168A) experimental SAS data
OTHER model
Sample: Interleukin-11 (W168A) monomer, 18 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Nov 28
Structures of the interleukin 11 signalling complex reveal gp130 dynamics and the inhibitory mechanism of a cytokine variant Nature Communications 14(1) (2023)
Metcalfe R, Hanssen E, Fung K, Aizel K, Kosasih C, Zlatic C, Doughty L, Morton C, Leis A, Parker M, Gooley P, Putoczki T, Griffin M
RgGuinier 1.7 nm
Dmax 5.2 nm
VolumePorod 22 nm3

SASDLR3 – Interleukin 11 Mutein

Interleukin 11 Mutein experimental SAS data
OTHER model
Sample: Interleukin 11 Mutein monomer, 18 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 8
Structures of the interleukin 11 signalling complex reveal gp130 dynamics and the inhibitory mechanism of a cytokine variant Nature Communications 14(1) (2023)
Metcalfe R, Hanssen E, Fung K, Aizel K, Kosasih C, Zlatic C, Doughty L, Morton C, Leis A, Parker M, Gooley P, Putoczki T, Griffin M
RgGuinier 1.8 nm
Dmax 5.4 nm
VolumePorod 25 nm3

SASDLS3 – Interleukin 11 Mutein, complex with gp130 (domains 1-3) and IL-11Rα

Interleukin-11 receptor subunit alphaInterleukin 11 MuteinInterleukin-6 receptor subunit beta experimental SAS data
DAMMIN model
Sample: Interleukin-11 receptor subunit alpha monomer, 32 kDa Homo sapiens protein
Interleukin 11 Mutein monomer, 18 kDa Homo sapiens protein
Interleukin-6 receptor subunit beta monomer, 35 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 8
Structures of the interleukin 11 signalling complex reveal gp130 dynamics and the inhibitory mechanism of a cytokine variant Nature Communications 14(1) (2023)
Metcalfe R, Hanssen E, Fung K, Aizel K, Kosasih C, Zlatic C, Doughty L, Morton C, Leis A, Parker M, Gooley P, Putoczki T, Griffin M
RgGuinier 4.4 nm
Dmax 15.6 nm
VolumePorod 160 nm3

SASDNW6 – AIP56, an AB-toxin from Photobacterium damselae subsp. piscicida

Apoptosis inducing protein experimental SAS data
OTHER model
Sample: Apoptosis inducing protein monomer, 57 kDa Photobacterium damselae subsp. … protein
Buffer: 50 mM Hepes, 500 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Apr 13
Unconventional structure and mechanisms for membrane interaction and translocation of the NF-κB-targeting toxin AIP56. Nat Commun 14(1):7431 (2023)
Lisboa J, Pereira C, Pinto RD, Rodrigues IS, Pereira LMG, Pinheiro B, Oliveira P, Pereira PJB, Azevedo JE, Durand D, Benz R, do Vale A, Dos Santos NMS
RgGuinier 2.8 nm
Dmax 9.5 nm
VolumePorod 76 nm3

SASDSN7 – Full length human mature gelsolin in closed state

Gelsolin experimental SAS data
GROMACS model
Sample: Gelsolin monomer, 85 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 100 mM NaCl, 1 mM EDTA, pH: 7.4
Experiment: SAXS data collected at B21, Diamond Light Source on 2020 Feb 24
Accurate and Efficient SAXS/SANS Implementation Including Solvation Layer Effects Suitable for Molecular Simulations. J Chem Theory Comput (2023)
Ballabio F, Paissoni C, Bollati M, de Rosa M, Capelli R, Camilloni C
RgGuinier 3.2 nm
Dmax 11.1 nm
VolumePorod 128 nm3

SASDJ95 – E3 ubiquitin-protein ligase BRE1 complexed with E2 ubiquitin conjugating enzyme RAD6

E3 ubiquitin-protein ligase BRE1Ubiquitin-conjugating enzyme E2 2 experimental SAS data
SREFLEX model
Sample: E3 ubiquitin-protein ligase BRE1 dimer, 50 kDa Saccharomyces cerevisiae (strain … protein
Ubiquitin-conjugating enzyme E2 2 monomer, 20 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 50 mM Tris, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Feb 11
Structural basis for the role of C-terminus acidic tail of Saccharomyces cerevisiae ubiquitin-conjugating enzyme (Rad6) in E3 ligase (Bre1) mediated recognition of histones International Journal of Biological Macromolecules :127717 (2023)
Yadav P, Gupta M, Wazahat R, Islam Z, Tsutakawa S, Kamthan M, Kumar P
RgGuinier 4.1 nm
Dmax 10.4 nm
VolumePorod 105 nm3

SASDJA5 – E2 ubiquitin conjugating enzyme RAD6

Ubiquitin-conjugating enzyme E2 2 experimental SAS data
SREFLEX model
Sample: Ubiquitin-conjugating enzyme E2 2 monomer, 20 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 50 mM Tris, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Feb 11
Structural basis for the role of C-terminus acidic tail of Saccharomyces cerevisiae ubiquitin-conjugating enzyme (Rad6) in E3 ligase (Bre1) mediated recognition of histones International Journal of Biological Macromolecules :127717 (2023)
Yadav P, Gupta M, Wazahat R, Islam Z, Tsutakawa S, Kamthan M, Kumar P
RgGuinier 2.3 nm
Dmax 6.6 nm
VolumePorod 31 nm3

SASDPQ5 – His-tagged L-methionine gamma-lyase from Clostridium tetani

L-methionine gamma-lyase experimental SAS data
CHIMERA model
Sample: L-methionine gamma-lyase tetramer, 181 kDa Clostridium tetani protein
Buffer: PBS-D2O: 137 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, 1.8 mM KH2PO4 (D2O buffer), pH: 7.4
Experiment: SANS data collected at YuMO SANS TOF spectrometer, IBR-2, Frank Laboratory of Neutron Physics, Joint Institute for Nuclear Research on 2019 May 19
Methionine gamma lyase fused with S3 domain VGF forms octamers and adheres to tumor cells via binding EGFR Biochemical and Biophysical Research Communications :149319 (2023)
Bondarev N, Bagaeva D, Bazhenov S, Buben M, Bulushova N, Ryzhykau Y, Okhrimenko I, Zagryadskaya Y, Maslov I, Anisimova N, Sokolova D, Kuklin A, Pokrovsky V, Manukhov I
RgGuinier 4.0 nm
Dmax 14.9 nm
VolumePorod 232 nm3