|
|
|
Sample: |
Histone-lysine N-methyltransferase 2A monomer, 25 kDa Homo sapiens protein
WD repeat-containing protein 5 monomer, 34 kDa Homo sapiens protein
Set1/Ash2 histone methyltransferase complex subunit ASH2 monomer, 60 kDa Homo sapiens protein
Retinoblastoma-binding protein 5 monomer, 53 kDa Homo sapiens protein
|
Buffer: |
300 mM NaCl, 25mM Tris-HCl, 4% glycerol, 1 mM TCEP, pH: 8
|
Experiment: |
SAXS
data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2019 Jun 22
|
The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex.
Nucleic Acids Res (2019)
Han J, Li T, Li Y, Li M, Wang X, Peng C, Su C, Li N, Li Y, Xu Y, Chen Y
|
RgGuinier |
5.3 |
nm |
Dmax |
17.2 |
nm |
VolumePorod |
313 |
nm3 |
|
|
|
|
|
Sample: |
Histone-lysine N-methyltransferase 2A monomer, 25 kDa Homo sapiens protein
WD repeat-containing protein 5 monomer, 34 kDa Homo sapiens protein
Set1/Ash2 histone methyltransferase complex subunit ASH2 monomer, 60 kDa Homo sapiens protein
Retinoblastoma-binding protein 5 monomer, 59 kDa Homo sapiens protein
|
Buffer: |
300 mM NaCl, 25mM Tris-HCl, 4% glycerol, 1 mM TCEP, pH: 8
|
Experiment: |
SAXS
data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2019 Jun 22
|
The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex.
Nucleic Acids Res (2019)
Han J, Li T, Li Y, Li M, Wang X, Peng C, Su C, Li N, Li Y, Xu Y, Chen Y
|
RgGuinier |
5.0 |
nm |
Dmax |
15.5 |
nm |
VolumePorod |
282 |
nm3 |
|
|
|
|
|
Sample: |
Enhanced disease susceptibility monomer, 72 kDa Arabidopsis thaliana protein
|
Buffer: |
50 mM NaCl, 50 mM HEPES, 1% glyercol, 1 mM DTT, pH: 8
|
Experiment: |
SAXS
data collected at BM29, ESRF on 2015 May 19
|
Arabidopsis immunity regulator EDS1 in a PAD4/SAG101-unbound form is a monomer with an inherently inactive conformation.
J Struct Biol :107390 (2019)
Voss M, Toelzer C, Bhandari DD, Parker JE, Niefind K
|
RgGuinier |
3.1 |
nm |
Dmax |
10.5 |
nm |
VolumePorod |
92 |
nm3 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|