Small Angle Scattering Biological Data Bank SASBDB

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7 hits found for Spiteri

SASDLX2 – Immunoglobulin G4 (IgG4) Deglycosylated

Immunoglobulin G subclass 4 experimental SAS data

Sample:	Immunoglobulin G subclass 4 monomer, 145 kDa Homo sapiens protein
Buffer:	20 mM L-histidine, 138 mM NaCl, and 2.6 mM KCl buffer, pH: 6
Experiment:	SAXS data collected at B21, Diamond Light Source on 2017 Oct 20

Using atomistic solution scattering modelling to elucidate the role of the Fc glycans in human IgG4. PLoS One 19(4):e0300964 (2024)
Spiteri VA, Doutch J, Rambo RP, Bhatt JS, Gor J, Dalby PA, Perkins SJ

R_g^Guinier	4.9	nm
D_max	16.9	nm
Volume^Porod	258	nm³

SASDLY2 – Immunoglobulin G4 (IgG4) Glycosylated

Sample:	Immunoglobulin G subclass 4 monomer, 145 kDa Homo sapiens protein
Buffer:	20 mM L-histidine, 138 mM NaCl, and 2.6 mM KCl buffer, pH: 6
Experiment:	SAXS data collected at B21, Diamond Light Source on 2017 Oct 20

R_g^Guinier	4.9	nm
D_max	16.3	nm
Volume^Porod	256	nm³

SASDLZ2 – Immunoglobulin G3 (IgG3) Glycosylated

Immunoglobulin G subclass 3 experimental SAS data

Sample:	Immunoglobulin G subclass 3 monomer, 155 kDa Homo sapiens protein
Buffer:	20 mM L-histidine, 138 mM NaCl, and 2.6 mM KCl buffer, pH: 6
Experiment:	SAXS data collected at B21, Diamond Light Source on 2019 Jul 29

Solution structures of human myeloma IgG3 antibody reveal extended Fab and Fc regions relative to the other IgG subclasses. J Biol Chem :100995 (2021)
Spiteri VA, Goodall M, Doutch J, Rambo RP, Gor J, Perkins SJ

R_g^Guinier	7.0	nm
D_max	22.9	nm
Volume^Porod	267	nm³

SASDL23 – Immunoglobulin G3 (IgG3) Deglycosylated

Sample:	Immunoglobulin G subclass 3 monomer, 155 kDa Homo sapiens protein
Buffer:	20 mM L-histidine, 138 mM NaCl, and 2.6 mM KCl buffer, pH: 6
Experiment:	SAXS data collected at B21, Diamond Light Source on 2019 Jul 29

R_g^Guinier	7.1	nm
D_max	27.7	nm
Volume^Porod	294	nm³

SASDNV5 – Botulinum Toxin E at acidic pH

Botulinum Toxin Serotype E, endonegative experimental SAS data

Sample:	Botulinum Toxin Serotype E, endonegative monomer, 144 kDa Clostridium botulinum protein
Buffer:	10 mM sodium acetate (20 mM ionic strength), pH: 4
Experiment:	SAXS data collected at B21, Diamond Light Source on 2019 Oct 6

Elucidation of critical pH-dependent structural changes in Botulinum Neurotoxin E. J Struct Biol :107876 (2022)
...Spiteri VA, Perkins SJ, Dalby PA

R_g^Guinier	4.3	nm
D_max	15.2	nm
Volume^Porod	240	nm³

SASDKB8 – Immunoglobulin G1 (IgG1) Glycosylated

Immunoglobulin G subclass 1 experimental SAS data

Sample:	Immunoglobulin G subclass 1 , 148 kDa Homo sapiens protein
Buffer:	20 mM L-histidine, 138 mM NaCl, and 2.6 mM KCl buffer, pH: 6
Experiment:	SAXS data collected at B21, Diamond Light Source on 2017 Oct 20

Solution structure of deglycosylated human IgG1 shows the role of CH2 glycans in its conformation Biophysical Journal (2021)
Spiteri V, Doutch J, Rambo R, Gor J, Dalby P, Perkins S

R_g^Guinier	5.1	nm
D_max	17.5	nm
Volume^Porod	269	nm³

SASDKC8 – Immunoglobulin G1 (IgG1) Deglycosylated

Sample:	Immunoglobulin G subclass 1 , 148 kDa Homo sapiens protein
Buffer:	20 mM L-histidine, 138 mM NaCl, and 2.6 mM KCl buffer, pH: 6
Experiment:	SAXS data collected at B21, Diamond Light Source on 2017 Oct 20

Solution structure of deglycosylated human IgG1 shows the role of CH2 glycans in its conformation Biophysical Journal (2021)
Spiteri V, Doutch J, Rambo R, Gor J, Dalby P, Perkins S

R_g^Guinier	5.2	nm
D_max	18.4	nm
Volume^Porod	271	nm³