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5 hits found for Tou

SASDU89 – Apolipoprotein A-I monomer, C-terminally truncated

Apolipoprotein A-I experimental SAS data
COOT model
Sample: Apolipoprotein A-I monomer, 22 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.1% sodium azide, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2021 Mar 20
The structure of the apolipoprotein A-I monomer provides insights into its oligomerisation and lipid-binding mechanisms Journal of Molecular Biology :169394 (2025)
Tou H, Rosenes Z, Khandokar Y, Zlatic C, Metcalfe R, Mok Y, Morton C, Gooley P, Griffin M
RgGuinier 2.3 nm
Dmax 7.9 nm
VolumePorod 27 nm3

SASDU99 – Apolipoprotein A-I dimer, C-terminally truncated

Apolipoprotein A-I experimental SAS data
DAMMIF model
Sample: Apolipoprotein A-I dimer, 43 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.1% sodium azide, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2021 Mar 20
The structure of the apolipoprotein A-I monomer provides insights into its oligomerisation and lipid-binding mechanisms Journal of Molecular Biology :169394 (2025)
Tou H, Rosenes Z, Khandokar Y, Zlatic C, Metcalfe R, Mok Y, Morton C, Gooley P, Griffin M
RgGuinier 4.2 nm
Dmax 14.0 nm
VolumePorod 58 nm3

SASDUA9 – Apolipoprotein A-I monomer, C-terminally truncated, triply methionine-oxidised

Apolipoprotein A-I experimental SAS data
Apolipoprotein A-I Kratky plot
Sample: Apolipoprotein A-I monomer, 22 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.1% sodium azide, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2023 Mar 1
The structure of the apolipoprotein A-I monomer provides insights into its oligomerisation and lipid-binding mechanisms Journal of Molecular Biology :169394 (2025)
Tou H, Rosenes Z, Khandokar Y, Zlatic C, Metcalfe R, Mok Y, Morton C, Gooley P, Griffin M
RgGuinier 2.5 nm
Dmax 8.0 nm
VolumePorod 32 nm3

SASDUB9 – Apolipoprotein A-I monomer, C-terminally truncated, SAXS construct G26R mutant

Apolipoprotein A-I (G50R) experimental SAS data
Apolipoprotein A-I (G50R) Kratky plot
Sample: Apolipoprotein A-I (G50R) monomer, 22 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.1% sodium azide, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2023 Jun 27
The structure of the apolipoprotein A-I monomer provides insights into its oligomerisation and lipid-binding mechanisms Journal of Molecular Biology :169394 (2025)
Tou H, Rosenes Z, Khandokar Y, Zlatic C, Metcalfe R, Mok Y, Morton C, Gooley P, Griffin M
RgGuinier 2.3 nm
Dmax 7.9 nm
VolumePorod 28 nm3

SASDUC9 – Full-length apolipoprotein A-I in complex with antigen-binding fragment 55201

Apolipoprotein A-IAntigen-binding fragment 55201 experimental SAS data
COOT model
Sample: Apolipoprotein A-I monomer, 28 kDa Homo sapiens protein
Antigen-binding fragment 55201 monomer, 45 kDa Mus musculus protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.1% sodium azide, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2021 Jun 19
The structure of the apolipoprotein A-I monomer provides insights into its oligomerisation and lipid-binding mechanisms Journal of Molecular Biology :169394 (2025)
Tou H, Rosenes Z, Khandokar Y, Zlatic C, Metcalfe R, Mok Y, Morton C, Gooley P, Griffin M
RgGuinier 4.6 nm
Dmax 17.5 nm
VolumePorod 99 nm3