Browse by MACROMOLECULE type: protein

SASDFB8 – Delta subunit of RNA polymerase, RNAP (B. subtilis): Lysine to glutamate mutant, 400mM NaCl

DNA-directed RNA polymerase subunit delta - mutant experimental SAS data
DNA-directed RNA polymerase subunit delta - mutant Kratky plot
Sample: DNA-directed RNA polymerase subunit delta - mutant monomer, 20 kDa Bacillus subtilis protein
Buffer: 20 mM Phosphate buffer, 400 mM NaCl, 0.05% NaN3, pH: 6.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Oct 3
Quantitative Conformational Analysis of Functionally Important Electrostatic Interactions in the Intrinsically Disordered Region of Delta Subunit of Bacterial RNA Polymerase. J Am Chem Soc (2019)
Kuban V, Srb P, Stegnerova H, Padrta P, Zachrdla M, Jasenakova Z, Šanderová H, Vítovská D, Krasny L, Koval T, Dohnalek J, Ziemska-Legi Cka J, Grynberg M, Jarnot P, Gruca A, Jensen MR, Blackledge M, Zidek L
RgGuinier 4.5 nm
Dmax 24.0 nm
VolumePorod 78 nm3

SASDFC8 – Delta subunit of RNA polymerase, RNAP (B. subtilis): Lysine to glutamate mutant, 800mM NaCl

DNA-directed RNA polymerase subunit delta - mutant experimental SAS data
DNA-directed RNA polymerase subunit delta - mutant Kratky plot
Sample: DNA-directed RNA polymerase subunit delta - mutant monomer, 20 kDa Bacillus subtilis protein
Buffer: 20 mM Phosphate buffer, 800 mM NaCl, 0.05% NaN3, pH: 6.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Oct 3
Quantitative Conformational Analysis of Functionally Important Electrostatic Interactions in the Intrinsically Disordered Region of Delta Subunit of Bacterial RNA Polymerase. J Am Chem Soc (2019)
Kuban V, Srb P, Stegnerova H, Padrta P, Zachrdla M, Jasenakova Z, Šanderová H, Vítovská D, Krasny L, Koval T, Dohnalek J, Ziemska-Legi Cka J, Grynberg M, Jarnot P, Gruca A, Jensen MR, Blackledge M, Zidek L
RgGuinier 4.5 nm
Dmax 21.0 nm
VolumePorod 74 nm3

SASDGD4 – Mixed lineage leukemia protein-1 complex, MLL1-WDR5-ASH2L-RBBP5(2-381)

Retinoblastoma-binding protein 5Histone-lysine N-methyltransferase 2AWD repeat-containing protein 5Set1/Ash2 histone methyltransferase complex subunit ASH2 experimental SAS data
Retinoblastoma-binding protein 5 Histone-lysine N-methyltransferase 2A WD repeat-containing protein 5 Set1/Ash2 histone methyltransferase complex subunit ASH2 Kratky plot
Sample: Retinoblastoma-binding protein 5 monomer, 42 kDa Homo sapiens protein
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
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 5.7 nm
Dmax 18.6 nm
VolumePorod 360 nm3

SASDGE4 – Mixed lineage leukemia protein-1 complex, MLL1-WDR5-ASH2L-RBBP5(2-480)

Histone-lysine N-methyltransferase 2AWD repeat-containing protein 5Set1/Ash2 histone methyltransferase complex subunit ASH2Retinoblastoma-binding protein 5 experimental SAS data
Histone-lysine N-methyltransferase 2A WD repeat-containing protein 5 Set1/Ash2 histone methyltransferase complex subunit ASH2 Retinoblastoma-binding protein 5 Kratky plot
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 5.0 nm
Dmax 15.3 nm
VolumePorod 256 nm3

SASDGF4 – Mixed lineage leukemia protein-1 complex, MLL1-WDR5-ASH2L-RBBP5(2-480)L399A/L400A/I457A/L459A

Histone-lysine N-methyltransferase 2AWD repeat-containing protein 5Set1/Ash2 histone methyltransferase complex subunit ASH2Retinoblastoma-binding protein 5 experimental SAS data
Histone-lysine N-methyltransferase 2A WD repeat-containing protein 5 Set1/Ash2 histone methyltransferase complex subunit ASH2 Retinoblastoma-binding protein 5 Kratky plot
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

SASDGG4 – Mixed lineage leukemia protein-1 complex, MLL1-WDR5-ASH2L-RBBP5(2-538)

Histone-lysine N-methyltransferase 2AWD repeat-containing protein 5Set1/Ash2 histone methyltransferase complex subunit ASH2Retinoblastoma-binding protein 5 experimental SAS data
Histone-lysine N-methyltransferase 2A WD repeat-containing protein 5 Set1/Ash2 histone methyltransferase complex subunit ASH2 Retinoblastoma-binding protein 5 Kratky plot
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

SASDFC5 – Enhanced disease susceptibility 1 (EDS1)

Enhanced disease susceptibility experimental SAS data
DAMMIN model
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

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

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)

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)

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