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9 hits found for Imamura

SASDW44 – Immunoglobulin G4 (pH 2, 0.2 M NaCl), SEC-SAXS data

humanized immunoglobulin G4 monoclonal antibody (lebrikizumab) experimental SAS data
humanized immunoglobulin G4 monoclonal antibody (lebrikizumab) Kratky plot
Sample: humanized immunoglobulin G4 monoclonal antibody (lebrikizumab) monomer, 148 kDa Mouse/human protein
Buffer: 100 mM glycine-HCl, 200 mM NaCl, pH: 2
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2024 Nov 19
IgG4 and IgG1 undergo common acid‐induced compaction into an alternatively folded state FEBS Letters (2025)
Imamura H, Honda S
RgGuinier 4.1 nm
Dmax 14.0 nm
VolumePorod 238 nm3

SASDW54 – Immunoglobulin G1 (pH 2, 0.2 M NaCl), SEC-SAXS data

humanized immunoglobulin G1 monoclonal antibody (trastuzumab) experimental SAS data
humanized immunoglobulin G1 monoclonal antibody (trastuzumab) Kratky plot
Sample: humanized immunoglobulin G1 monoclonal antibody (trastuzumab) monomer, 148 kDa Mouse/human protein
Buffer: 100 mM glycine-HCl, 200 mM NaCl, pH: 2
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2023 May 20
IgG4 and IgG1 undergo common acid‐induced compaction into an alternatively folded state FEBS Letters (2025)
Imamura H, Honda S
RgGuinier 4.2 nm
Dmax 12.9 nm
VolumePorod 240 nm3

SASDW64 – Immunoglobulin G4 (pH 7)

humanized immunoglobulin G4 monoclonal antibody (lebrikizumab) experimental SAS data
humanized immunoglobulin G4 monoclonal antibody (lebrikizumab) Kratky plot
Sample: humanized immunoglobulin G4 monoclonal antibody (lebrikizumab) monomer, 148 kDa Mouse/human protein
Buffer: 10 mM sodium phosphate, pH: 7
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2024 Nov 19
IgG4 and IgG1 undergo common acid‐induced compaction into an alternatively folded state FEBS Letters (2025)
Imamura H, Honda S
RgGuinier 4.8 nm
Dmax 15.6 nm
VolumePorod 211 nm3

SASDNK7 – Guanine-rich DNA derived from the promoter region of c-MYC gene (MYC22-G14T/G23T) with KCl

MYC22-G14T/G23T experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: MYC22-G14T/G23T monomer, 7 kDa Homo sapiens DNA
Buffer: 50 mM Tris, 30 mM KCl, pH: 8
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2022 Feb 27
Small-angle X-ray scattering data of a guanine-rich DNA derived from the promoter region of c-MYC gene in solution Data in Brief :108285 (2022)
...Imamura H, Yamaoki Y, Kato M
RgGuinier 1.3 nm
Dmax 5.3 nm
VolumePorod 9 nm3

SASDNL7 – Guanine-rich DNA derived from the promoter region of c-MYC gene (MYC22-G14T/G23T) with 18-crown-6

MYC22-G14T/G23T experimental SAS data
MYC22-G14T/G23T Kratky plot
Sample: MYC22-G14T/G23T monomer, 7 kDa Homo sapiens DNA
Buffer: 50 mM Tris, 100 mM 18-crown-6, pH: 8
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2022 Feb 27
Small-angle X-ray scattering data of a guanine-rich DNA derived from the promoter region of c-MYC gene in solution Data in Brief :108285 (2022)
...Imamura H, Yamaoki Y, Kato M
RgGuinier 1.6 nm
Dmax 6.0 nm
VolumePorod 10 nm3

SASDDG2 – Glycosylated Human Immunoglobulin G Fc Region

Glycosylated human immunoglobulin G Fc region experimental SAS data
MODELLER model
Sample: Glycosylated human immunoglobulin G Fc region dimer, 53 kDa Homo sapiens protein
Buffer: 20 mM Citrate-Phosphate, pH: 7
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2017 Mar 5
CH2 domain orientation of human immunoglobulin G in solution: Structural comparison of glycosylated and aglycosylated Fc regions using small-angle X-ray scattering. MAbs (2018)
...Imamura H, Shibuya R, Honda S
RgGuinier 2.7 nm
Dmax 10.2 nm
VolumePorod 66 nm3

SASDDH2 – Aglycosylated Human Immunoglobulin G Fc Region

Aglycosylated human immunoglobulin G Fc region experimental SAS data
MODELLER model
Sample: Aglycosylated human immunoglobulin G Fc region dimer, 51 kDa Homo sapiens protein
Buffer: 20 mM Citrate-Phosphate, pH: 7
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2017 Mar 5
CH2 domain orientation of human immunoglobulin G in solution: Structural comparison of glycosylated and aglycosylated Fc regions using small-angle X-ray scattering. MAbs (2018)
...Imamura H, Shibuya R, Honda S
RgGuinier 2.9 nm
Dmax 9.8 nm
VolumePorod 60 nm3

SASDQ99 – Immunoglobulin G1 (pH 2, 0 M NaCl), SEC-SAXS data

humanized immunoglobulin G1 monoclonal antibody experimental SAS data
humanized immunoglobulin G1 monoclonal antibody Kratky plot
Sample: humanized immunoglobulin G1 monoclonal antibody monomer, 148 kDa Mouse/human (chimera)
Buffer: 100 mM glycine-HCl, pH: 2
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2016 Mar 2
Getting Smaller by Denaturation: Acid-Induced Compaction of Antibodies The Journal of Physical Chemistry Letters :3898-3906 (2023)
Imamura H, Ooishi A, Honda S
RgGuinier 5.1 nm
Dmax 17.6 nm
VolumePorod 260 nm3

SASDQA9 – Immunoglobulin G1 (pH 2, 0.2 M NaCl), SEC-SAXS data

humanized immunoglobulin G1 monoclonal antibody experimental SAS data
humanized immunoglobulin G1 monoclonal antibody Kratky plot
Sample: humanized immunoglobulin G1 monoclonal antibody monomer, 148 kDa Mouse/human (chimera)
Buffer: 100 mM glycine-HCl, 200 mM NaCl, pH: 2
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2017 Mar 5
Getting Smaller by Denaturation: Acid-Induced Compaction of Antibodies The Journal of Physical Chemistry Letters :3898-3906 (2023)
Imamura H, Ooishi A, Honda S
RgGuinier 4.1 nm
Dmax 14.2 nm
VolumePorod 240 nm3