SASDWV2 – Human immunoglobulin gamma 1 (IgG1) SAP1.3

Human immunoglobulin gamma 1 (IgG1) SAP1.3 - heavy chainHuman immunoglobulin SAP1.3 - kappa chain experimental SAS data
Human immunoglobulin gamma 1 (IgG1) SAP1.3 - heavy chain Human immunoglobulin SAP1.3 - kappa chain Kratky plot
Sample: Human immunoglobulin gamma 1 (IgG1) SAP1.3 - heavy chain dimer, 99 kDa Homo sapiens protein
Human immunoglobulin SAP1.3 - kappa chain dimer, 48 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 150 mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2024 Sep 28
Structure-guided disulfide engineering restricts antibody conformation to elicit TNFR agonism. Nat Commun 16(1):3495 (2025)
Elliott IG, Fisher H, Chan HTC, Inzhelevskaya T, Mockridge CI, Penfold CA, Duriez PJ, Orr CM, Herniman J, Müller KTJ, Essex JW, Cragg MS, Tews I
RgGuinier 5.2 nm
Dmax 16.8 nm
VolumePorod 229 nm3

SASDWW2 – Human immunoglobulin gamma 2 (IgG2) SAP1.3

Human immunoglobulin SAP1.3 - kappa chainHuman immunoglobulin gamma 2 (IgG2) SAP1.3 - heavy chain experimental SAS data
Human immunoglobulin SAP1.3 - kappa chain Human immunoglobulin gamma 2 (IgG2) SAP1.3 - heavy chain Kratky plot
Sample: Human immunoglobulin SAP1.3 - kappa chain dimer, 48 kDa Homo sapiens protein
Human immunoglobulin gamma 2 (IgG2) SAP1.3 - heavy chain dimer, 99 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 150 mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2024 Sep 28
Structure-guided disulfide engineering restricts antibody conformation to elicit TNFR agonism. Nat Commun 16(1):3495 (2025)
Elliott IG, Fisher H, Chan HTC, Inzhelevskaya T, Mockridge CI, Penfold CA, Duriez PJ, Orr CM, Herniman J, Müller KTJ, Essex JW, Cragg MS, Tews I
RgGuinier 4.9 nm
Dmax 15.9 nm
VolumePorod 214 nm3

SASDWX2 – Human immunoglobulin gamma 2 (IgG2) SAP1.3 - heavy chain C226S kappa chain C214S mutant

Human immunoglobulin gamma 2 (IgG2) SAP1.3 - heavy chain C226SHuman immunoglobulin SAP1.3 - kappa chain C214S experimental SAS data
Human immunoglobulin gamma 2 (IgG2) SAP1.3 - heavy chain C226S Human immunoglobulin SAP1.3 - kappa chain C214S Kratky plot
Sample: Human immunoglobulin gamma 2 (IgG2) SAP1.3 - heavy chain C226S dimer, 99 kDa Homo sapiens protein
Human immunoglobulin SAP1.3 - kappa chain C214S dimer, 48 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 150 mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2024 Sep 28
Structure-guided disulfide engineering restricts antibody conformation to elicit TNFR agonism. Nat Commun 16(1):3495 (2025)
Elliott IG, Fisher H, Chan HTC, Inzhelevskaya T, Mockridge CI, Penfold CA, Duriez PJ, Orr CM, Herniman J, Müller KTJ, Essex JW, Cragg MS, Tews I
RgGuinier 4.9 nm
Dmax 15.8 nm
VolumePorod 213 nm3

SASDWY2 – Human immunoglobulin gamma 2 (IgG2) SAP1.3 - heavy chain C227S kappa chain C214S mutant

Human immunoglobulin SAP1.3 - kappa chain C214SHuman immunoglobulin gamma 2 (IgG2) SAP1.3 - heavy chain C227S experimental SAS data
Human immunoglobulin SAP1.3 - kappa chain C214S Human immunoglobulin gamma 2 (IgG2) SAP1.3 - heavy chain C227S Kratky plot
Sample: Human immunoglobulin SAP1.3 - kappa chain C214S dimer, 48 kDa Homo sapiens protein
Human immunoglobulin gamma 2 (IgG2) SAP1.3 - heavy chain C227S dimer, 99 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 150 mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2024 Sep 28
Structure-guided disulfide engineering restricts antibody conformation to elicit TNFR agonism. Nat Commun 16(1):3495 (2025)
Elliott IG, Fisher H, Chan HTC, Inzhelevskaya T, Mockridge CI, Penfold CA, Duriez PJ, Orr CM, Herniman J, Müller KTJ, Essex JW, Cragg MS, Tews I
RgGuinier 4.9 nm
Dmax 15.7 nm
VolumePorod 222 nm3

SASDWZ2 – Human immunoglobulin gamma 2 (IgG2) SAP1.3 - heavy chain C226S/C227S mutant

Human immunoglobulin SAP1.3 - kappa chainHuman immunoglobulin gamma 2 (IgG2) SAP1.3 - heavy chain C226S/C227S experimental SAS data
Human immunoglobulin SAP1.3 - kappa chain Human immunoglobulin gamma 2 (IgG2) SAP1.3 - heavy chain C226S/C227S Kratky plot
Sample: Human immunoglobulin SAP1.3 - kappa chain dimer, 48 kDa Homo sapiens protein
Human immunoglobulin gamma 2 (IgG2) SAP1.3 - heavy chain C226S/C227S dimer, 99 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 150 mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2024 Sep 28
Structure-guided disulfide engineering restricts antibody conformation to elicit TNFR agonism. Nat Commun 16(1):3495 (2025)
Elliott IG, Fisher H, Chan HTC, Inzhelevskaya T, Mockridge CI, Penfold CA, Duriez PJ, Orr CM, Herniman J, Müller KTJ, Essex JW, Cragg MS, Tews I
RgGuinier 5.0 nm
Dmax 15.8 nm
VolumePorod 222 nm3

SASDSC7 – Human immunoglobulin gamma 2 (IgG2) ChiLob 7/4 F(ab')2 - heavy chain T219C/C224S kappa chain E123C/C214S

Human immunoglobulin gamma 2 (IgG2) ChiLob 7/4 F(ab')2 - heavy chain T219C/C224SHuman immunoglobulin gamma 2 (IgG2) ChiLob 7/4 F(ab')2 - kappa chain E123C/C214S experimental SAS data
Human immunoglobulin gamma 2 (IgG2) ChiLob 7/4 F(ab')2 - heavy chain T219C/C224S kappa chain E123C/C214S Rg histogram
Sample: Human immunoglobulin gamma 2 (IgG2) ChiLob 7/4 F(ab')2 - heavy chain T219C/C224S dimer, 52 kDa protein
Human immunoglobulin gamma 2 (IgG2) ChiLob 7/4 F(ab')2 - kappa chain E123C/C214S dimer, 47 kDa protein
Buffer: 50 mM HEPES, 150 mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2022 Apr 12
Structure-guided disulfide engineering restricts antibody conformation to elicit TNFR agonism. Nat Commun 16(1):3495 (2025)
Elliott IG, Fisher H, Chan HTC, Inzhelevskaya T, Mockridge CI, Penfold CA, Duriez PJ, Orr CM, Herniman J, Müller KTJ, Essex JW, Cragg MS, Tews I
RgGuinier 3.9 nm
Dmax 13.2 nm
VolumePorod 124 nm3

SASDSD7 – Human immunoglobulin gamma 2 (IgG2) ChiLob 7/4 F(ab')2 - heavy chain K223C/C224S kappa chain C214S

Human immunoglobulin gamma 2 (IgG2) ChiLob 7/4 F(ab')2 - heavy chain K223C/C224SHuman immunoglobulin gamma 2 (IgG2) ChiLob 7/4 F(ab')2 - kappa light chain C214S experimental SAS data
Human immunoglobulin gamma 2 (IgG2) ChiLob 7/4 F(ab')2 - heavy chain K223C/C224S kappa chain C214S Rg histogram
Sample: Human immunoglobulin gamma 2 (IgG2) ChiLob 7/4 F(ab')2 - heavy chain K223C/C224S dimer, 52 kDa protein
Human immunoglobulin gamma 2 (IgG2) ChiLob 7/4 F(ab')2 - kappa light chain C214S dimer, 47 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 150 mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2022 Apr 12
Structure-guided disulfide engineering restricts antibody conformation to elicit TNFR agonism. Nat Commun 16(1):3495 (2025)
Elliott IG, Fisher H, Chan HTC, Inzhelevskaya T, Mockridge CI, Penfold CA, Duriez PJ, Orr CM, Herniman J, Müller KTJ, Essex JW, Cragg MS, Tews I
RgGuinier 3.9 nm
Dmax 13.2 nm
VolumePorod 124 nm3

SASDW74 – Aromatic-L-amino-acid decarboxylase L353P bound to pyridoxal 5'-phosphate (PLP)

Aromatic-L-amino-acid decarboxylase (L353P) experimental SAS data
DAMMIN model
Sample: Aromatic-L-amino-acid decarboxylase (L353P) dimer, 107 kDa Homo sapiens protein
Buffer: 50 mM HEPES, pH: 7.4
Experiment: SAXS data collected at B21, Diamond Light Source on 2021 Jul 7
Aromatic-L-amino-acid decarboxylase (AADC) L353P - pyridoxal 5'-phosphate bound form
Benny Danilo Belviso
RgGuinier 3.1 nm
Dmax 8.8 nm
VolumePorod 152 nm3

SASDW84 – Aromatic-L-amino-acid decarboxylase R347Q bound to pyridoxal 5'-phosphate (PLP)

Aromatic-L-amino-acid decarboxylase (R347Q) experimental SAS data
DAMMIN model
Sample: Aromatic-L-amino-acid decarboxylase (R347Q) dimer, 108 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 100 µM pyridoxal 5'-phosphate, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2021 Jul 7
Aromatic-L-amino-acid decarboxylase (AADC) L353P - pyridoxal 5'-phosphate bound form
Benny Danilo Belviso
RgGuinier 3.6 nm
Dmax 14.2 nm
VolumePorod 220 nm3

SASDW97 – Recombination directionality factor (6H-RdfS) from M.japonicum bound to 40mer DNA

Recombination directionality factor RdfSattP_8 40-mer DNA experimental SAS data
OTHER model
Sample: Recombination directionality factor RdfS tetramer, 52 kDa Mesorhizobium japonicum R7A protein
attP_8 40-mer DNA dimer, 25 kDa DNA
Buffer: 150 mM Tris-HCl, 300 mM NaCl, 5% v/v glycerol, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 19
Structural basis for control of integrative and conjugative element excision and transfer by the oligomeric winged helix–turn–helix protein RdfS Nucleic Acids Research 53(6) (2025)
Verdonk C, Agostino M, Eto K, Hall D, Bond C, Ramsay J
RgGuinier 3.8 nm
Dmax 13.8 nm
VolumePorod 134 nm3

4690 hits found.