SASBDB entries for UniProt ID: P78352

SASDGB5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) bound to RRESEI peptide

UniProt ID: P78352 (55-249) PDZ1-2 fragment of PSD-95/Disks large homolog 4
PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 10 mM RRESEI, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 11
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 3.0 nm
Dmax 13.1 nm
VolumePorod 32 nm3

SASDGC5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) bound to RRESEI peptide (diluted)

UniProt ID: P78352 (55-249) PDZ1-2 fragment of PSD-95/Disks large homolog 4
PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 5 mM RRESEI, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 11
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.6 nm
Dmax 12.4 nm
VolumePorod 32 nm3

SASDGD5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) bound to RRESEI peptide (Paused SEC)

UniProt ID: P78352 (55-249) PDZ1-2 fragment of PSD-95/Disks large homolog 4
PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 10 mM RRESEI, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jan 26
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.3 nm
Dmax 6.8 nm
VolumePorod 28 nm3

SASDGE5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95)

UniProt ID: P78352 (55-249) PDZ1-2 fragment of PSD-95/Disks large homolog 4
PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 11
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.4 nm
Dmax 9.2 nm
VolumePorod 32 nm3

SASDGF5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) (diluted)

UniProt ID: P78352 (55-249) PDZ1-2 fragment of PSD-95/Disks large homolog 4
PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 11
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.5 nm
Dmax 9.5 nm
VolumePorod 32 nm3

SASDGG5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) (Paused SEC)

UniProt ID: P78352 (55-249) PDZ1-2 fragment of PSD-95/Disks large homolog 4
PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jan 26
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.4 nm
Dmax 6.4 nm
VolumePorod 31 nm3

SASDGH5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) + glutathione (GSH)

UniProt ID: P78352 (55-249) PDZ1-2 fragment of PSD-95/Disks large homolog 4
PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 10 mM GSH, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Sep 16
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.7 nm
Dmax 6.3 nm
VolumePorod 29 nm3

SASDGJ5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) + glutathione (GSH) (diluted)

UniProt ID: P78352 (55-249) PDZ1-2 fragment of PSD-95/Disks large homolog 4
PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 16 mM GSH, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Sep 16
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 3.1 nm
Dmax 7.0 nm
VolumePorod 41 nm3

SASDGK5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) + glutathione (GSH) (Paused SEC)

UniProt ID: P78352 (55-249) PDZ1-2 fragment of PSD-95/Disks large homolog 4
PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 10 mM GSH, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jan 26
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.4 nm
Dmax 7.2 nm
VolumePorod 30 nm3