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13 hits found for Apolipoprotein A-I

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
...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

SASDC99 – Nanolipoprotein Particle (NLP) from In Vitro Assembly - 100% D2O SANS

Apolipoprotein A-I1,2-dimyristoyl-sn-glycero-3-phosphocholine experimental SAS data
Apolipoprotein A-I 1,2-dimyristoyl-sn-glycero-3-phosphocholine Kratky plot
Sample: Apolipoprotein A-I dimer, 50 kDa Mus musculus protein
1,2-dimyristoyl-sn-glycero-3-phosphocholine , 92 kDa
Buffer: PBS in D2O, pH: 7.4
Experiment: SANS data collected at NG7, NIST Center for High Resolution Neutron Scattering (CHRNS) on 2015 Nov 25
Small-angle X-ray and neutron scattering demonstrates that cell-free expression produces properly formed disc-shaped nanolipoprotein particles. Protein Sci 27(3):780-789 (2018)
Cleveland TE 4th, He W, Evans AC, Fischer NO, Lau EY, Coleman MA, Butler P
RgGuinier 3.1 nm
Dmax 9.1 nm

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
...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

SASDCA9 – Nanolipoprotein Particle (NLP) from In Vitro Assembly - SAXS

Apolipoprotein A-I1,2-dimyristoyl-sn-glycero-3-phosphocholine experimental SAS data
Apolipoprotein A-I 1,2-dimyristoyl-sn-glycero-3-phosphocholine Kratky plot
Sample: Apolipoprotein A-I dimer, 50 kDa Mus musculus protein
1,2-dimyristoyl-sn-glycero-3-phosphocholine , 92 kDa
Buffer: PBS in D2O, pH: 7.4
Experiment: SAXS data collected at SAXSLab Bio-Ganesha, Institute for Bioscience and Biotechnology Research, National Institute of Standards and Technology (IBBR/NIST) on 2015 Nov 24
Small-angle X-ray and neutron scattering demonstrates that cell-free expression produces properly formed disc-shaped nanolipoprotein particles. Protein Sci 27(3):780-789 (2018)
Cleveland TE 4th, He W, Evans AC, Fischer NO, Lau EY, Coleman MA, Butler P
RgGuinier 4.8 nm
Dmax 12.0 nm

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
...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

SASDCB9 – Nanolipoprotein Particle (NLP) assembled with tail-deuterated DMPC - 100% D2O SANS

Apolipoprotein A-I1,2-dimyristoyl-d54-sn-glycero-3-phosphocholine experimental SAS data
Apolipoprotein A-I 1,2-dimyristoyl-d54-sn-glycero-3-phosphocholine Kratky plot
Sample: Apolipoprotein A-I dimer, 50 kDa Mus musculus protein
1,2-dimyristoyl-d54-sn-glycero-3-phosphocholine , 99 kDa
Buffer: PBS in D2O, pH: 7.4
Experiment: SANS data collected at NG7, NIST Center for High Resolution Neutron Scattering (CHRNS) on 2016 Apr 11
Small-angle X-ray and neutron scattering demonstrates that cell-free expression produces properly formed disc-shaped nanolipoprotein particles. Protein Sci 27(3):780-789 (2018)
Cleveland TE 4th, He W, Evans AC, Fischer NO, Lau EY, Coleman MA, Butler P
RgGuinier 4.3 nm
Dmax 10.7 nm

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
...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

SASDCC9 – Nanolipoprotein Particle (NLP) from In Vitro Assembly - 42% D2O SANS

Apolipoprotein A-I1,2-dimyristoyl-sn-glycero-3-phosphocholine experimental SAS data
Apolipoprotein A-I 1,2-dimyristoyl-sn-glycero-3-phosphocholine Kratky plot
Sample: Apolipoprotein A-I dimer, 50 kDa Mus musculus protein
1,2-dimyristoyl-sn-glycero-3-phosphocholine , 92 kDa
Buffer: PBS in 42% D2O, pH: 7.4
Experiment: SANS data collected at NGB 30m SANS, NIST Center for High Resolution Neutron Scattering (CHRNS) on 2015 Dec 11
Small-angle X-ray and neutron scattering demonstrates that cell-free expression produces properly formed disc-shaped nanolipoprotein particles. Protein Sci 27(3):780-789 (2018)
Cleveland TE 4th, He W, Evans AC, Fischer NO, Lau EY, Coleman MA, Butler P
RgGuinier 2.9 nm
Dmax 7.3 nm

SASDUC9 – ...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
...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

SASDCD9 – Nanolipoprotein Particle (NLP) from Cell-Free Expression - SAXS

1,2-dimyristoyl-sn-glycero-3-phosphocholineApolipoprotein A-I experimental SAS data
1,2-dimyristoyl-sn-glycero-3-phosphocholine Apolipoprotein A-I Kratky plot
Sample: 1,2-dimyristoyl-sn-glycero-3-phosphocholine , 92 kDa
Apolipoprotein A-I dimer, 52 kDa Mus musculus protein
Buffer: PBS in D2O, pH: 7.4
Experiment: SAXS data collected at SAXSLab Bio-Ganesha, Institute for Bioscience and Biotechnology Research, National Institute of Standards and Technology (IBBR/NIST) on 2015 Nov 24
Small-angle X-ray and neutron scattering demonstrates that cell-free expression produces properly formed disc-shaped nanolipoprotein particles. Protein Sci 27(3):780-789 (2018)
Cleveland TE 4th, He W, Evans AC, Fischer NO, Lau EY, Coleman MA, Butler P
RgGuinier 4.7 nm
Dmax 12.7 nm

SASDCE9 – Nanolipoprotein Particle (NLP) with Telodendrimer - SAXS

1,2-dimyristoyl-sn-glycero-3-phosphocholineApolipoprotein A-I experimental SAS data
1,2-dimyristoyl-sn-glycero-3-phosphocholine Apolipoprotein A-I Kratky plot
Sample: 1,2-dimyristoyl-sn-glycero-3-phosphocholine , 92 kDa
Apolipoprotein A-I dimer, 52 kDa Mus musculus protein
Buffer: PBS in D2O, pH: 7.4
Experiment: SAXS data collected at SAXSLab Bio-Ganesha, Institute for Bioscience and Biotechnology Research, National Institute of Standards and Technology (IBBR/NIST) on 2015 Nov 24
Small-angle X-ray and neutron scattering demonstrates that cell-free expression produces properly formed disc-shaped nanolipoprotein particles. Protein Sci 27(3):780-789 (2018)
Cleveland TE 4th, He W, Evans AC, Fischer NO, Lau EY, Coleman MA, Butler P
RgGuinier 4.4 nm
Dmax 12.7 nm

SASDCF9 – Nanolipoprotein Particle (NLP) from Cell-Free Expression - 100% D2O SANS

1,2-dimyristoyl-sn-glycero-3-phosphocholineApolipoprotein A-I experimental SAS data
1,2-dimyristoyl-sn-glycero-3-phosphocholine Apolipoprotein A-I Kratky plot
Sample: 1,2-dimyristoyl-sn-glycero-3-phosphocholine , 92 kDa
Apolipoprotein A-I dimer, 52 kDa Mus musculus protein
Buffer: PBS in D2O, pH: 7.4
Experiment: SANS data collected at NG7, NIST Center for High Resolution Neutron Scattering (CHRNS) on 2015 Nov 25
Small-angle X-ray and neutron scattering demonstrates that cell-free expression produces properly formed disc-shaped nanolipoprotein particles. Protein Sci 27(3):780-789 (2018)
Cleveland TE 4th, He W, Evans AC, Fischer NO, Lau EY, Coleman MA, Butler P
RgGuinier 3.5 nm
Dmax 12.5 nm

SASDCG9 – Nanolipoprotein Particle (NLP) with Telodendrimer - 100% D2O SANS

1,2-dimyristoyl-sn-glycero-3-phosphocholineApolipoprotein A-I experimental SAS data
1,2-dimyristoyl-sn-glycero-3-phosphocholine Apolipoprotein A-I Kratky plot
Sample: 1,2-dimyristoyl-sn-glycero-3-phosphocholine , 92 kDa
Apolipoprotein A-I dimer, 52 kDa Mus musculus protein
Buffer: PBS in D2O, pH: 7.4
Experiment: SANS data collected at NG7, NIST Center for High Resolution Neutron Scattering (CHRNS) on 2015 Nov 25
Small-angle X-ray and neutron scattering demonstrates that cell-free expression produces properly formed disc-shaped nanolipoprotein particles. Protein Sci 27(3):780-789 (2018)
Cleveland TE 4th, He W, Evans AC, Fischer NO, Lau EY, Coleman MA, Butler P
RgGuinier 3.3 nm
Dmax 10.0 nm