Conformational Plasticity of the Immunoglobulin Fc Domain in Solution.

Remesh SG, Armstrong AA, Mahan AD, Luo J, Hammel M
Structure 26(7):1007-1014.e2 (2018 Jul 3)
PMID: 29731233
doi: 10.1016/j.str.2018.03.017
Submitted to SASBDB: 2018 Mar 6
Published in SASBDB:

SASDDT4 – Fc region of Immunoglobulin G1 (IgG1 Fc)

Immunoglobulin heavy constant gamma 1 experimental SAS data
BILBOMD model
Sample: Immunoglobulin heavy constant gamma 1 dimer, 53 kDa Homo sapiens protein
Buffer: 20mM HEPES, 50mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Feb 17
RgGuinier 2.6 nm
Dmax 10.0 nm
VolumePorod 70 nm3

SASDDU4 – Fc region of Immunoglobulin G2 (IgG2 Fc)

Immunoglobulin heavy constant gamma 2 experimental SAS data
BILBOMD model
Sample: Immunoglobulin heavy constant gamma 2 dimer, 52 kDa Homo sapiens protein
Buffer: 20mM HEPES, 50mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Feb 17
RgGuinier 2.8 nm
Dmax 9.0 nm
VolumePorod 67 nm3

SASDDV4 – Fc-region of Immunoglobulin G1, M135Y/S137T/T139E mutant (IgG1 Fc-YTE)

Immunoglobulin heavy constant gamma 1 M255Y/S257T/T259E experimental SAS data
BILBOMD model
Sample: Immunoglobulin heavy constant gamma 1 M255Y/S257T/T259E dimer, 53 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 50mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Feb 17
RgGuinier 2.7 nm
Dmax 10.0 nm
VolumePorod 74 nm3