Search

  
Advanced search  

7 hits found for Heidar Koning

SASDXD4 – Full-length human SFPQ dimer (protiated and deuterated)

Splicing factor, proline- and glutamine-rich experimental SAS data
Splicing factor, proline- and glutamine-rich Kratky plot
Sample: Splicing factor, proline- and glutamine-rich dimer, 153 kDa Homo sapiens protein
Buffer: 150 mM KCl, 1.5% glycerol, 20 mM HEPES, 1 mM DTT (in 100% H2O), pH: 7.4
Experiment: SANS data collected at Quokka - Small Angle Neutron Scattering, Australian Centre for Neutron Scattering (ANSTO) on 2023 Jan 23
Dimers of full-length SFPQ observed by SANS
Heidar Koning
RgGuinier 8.7 nm
Dmax 30.7 nm
VolumePorod 241000 nm3

SASDV67 – Human Splicing Factor Proline/Glutamine rich SFPQ1 dimer with C-terminal truncation (delta599-707)

Splicing Factor Proline/Glutamine rich (1-598) experimental SAS data
Splicing Factor Proline/Glutamine rich (1-598) Kratky plot
Sample: Splicing Factor Proline/Glutamine rich (1-598) dimer, 130 kDa Homo sapiens protein
Buffer: 500mM KNO3, 20mM HEPES, 5% glycerol, 1mM DTT, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2023 Mar 13
Full-length SFPQ, and SFPQ1-598 homodimers
Heidar Koning
RgGuinier 7.6 nm
Dmax 34.3 nm
VolumePorod 400 nm3

SASDV77 – Human Splicing Factor Proline/Glutamine rich SFPQ1 dimer with C-terminal truncation (delta599-707) in low salt buffer

Splicing Factor Proline/Glutamine rich (1-598) experimental SAS data
Splicing Factor Proline/Glutamine rich (1-598) Kratky plot
Sample: Splicing Factor Proline/Glutamine rich (1-598) dimer, 130 kDa Homo sapiens protein
Buffer: 150 mM KCl, 20 mM HEPES, 5% glycerol, 5 mM MgCl2, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2023 Mar 13
Full-length SFPQ, and SFPQ1-598 homodimers
Heidar Koning
RgGuinier 6.1 nm
Dmax 28.0 nm
VolumePorod 315 nm3

SASDV59 – Human Splicing factor, proline- and glutamine-rich protein 5% SFPQ and 95% dSFPQ at a D2O matchpoint of 95%

Splicing factor, proline- and glutamine-rich experimental SAS data
Splicing factor, proline- and glutamine-rich Kratky plot
Sample: Splicing factor, proline- and glutamine-rich dimer, 153 kDa Homo sapiens protein
Buffer: 150 mM KCl, 0.075% glycerol, 20 mM HEPES, 0.5 mM DTT,, pH: 7.4
Experiment: SANS data collected at Quokka - Small Angle Neutron Scattering, Australian Centre for Neutron Scattering (ANSTO) on 2023 Jan 20
Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation
Heidar Koning
RgGuinier 6.1 nm
Dmax 22.0 nm
VolumePorod 181 nm3

SASDMV7 – The tetramer of splicing factor, proline- and glutamine-rich and Non-POU domain-containing octamer-binding protein (SFPQ214-598(R542C)/NONO53-312)

Splicing factor, proline- and glutamine-richNon-POU domain-containing octamer-binding protein experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Splicing factor, proline- and glutamine-rich dimer, 153 kDa Homo sapiens protein
Non-POU domain-containing octamer-binding protein dimer, 60 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 7.5, 250 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 18
Structural plasticity of the coiled-coil interactions in human SFPQ. Nucleic Acids Res (2024)
Koning HJ, Lai JY, Marshall AC, Stroeher E, Monahan G, Pullakhandam A, Knott GJ, Ryan TM, Fox AH, Whitten A, Lee M, Bond CS
RgGuinier 5.5 nm
Dmax 20.4 nm
VolumePorod 304 nm3

SASDMW8 – The disulphide-linked tetramer of splicing factor, proline- and glutamine-rich and Non-POU domain-containing octamer-binding protein (SFPQ276-598(R542C)/NONO53-312) at 0.78mg/ml

Non-POU domain-containing octamer-binding proteinSplicing factor, proline- and glutamine-rich SFPQ276-598(R542C)/NONO53-312 dimer) experimental SAS data
DAMMIF model
Sample: Non-POU domain-containing octamer-binding protein dimer, 60 kDa Homo sapiens protein
Splicing factor, proline- and glutamine-rich SFPQ276-598(R542C)/NONO53-312 dimer) dimer, 76 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 7.5, 250 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Apr 28
Structural plasticity of the coiled-coil interactions in human SFPQ. Nucleic Acids Res (2024)
Koning HJ, Lai JY, Marshall AC, Stroeher E, Monahan G, Pullakhandam A, Knott GJ, Ryan TM, Fox AH, Whitten A, Lee M, Bond CS
RgGuinier 5.2 nm
Dmax 21.0 nm
VolumePorod 257 nm3

SASDMW7 – Concentration dependent dimer-tetramer transition of splicing factor, proline- and glutamine-rich with Non-POU domain-containing octamer-binding protein (SFPQ276-565/NONO53-312)

Splicing factor, proline- and glutamine-rich (276-565)Non-POU domain-containing octamer-binding protein (53-312) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Splicing factor, proline- and glutamine-rich (276-565) monomer, 34 kDa Homo sapiens protein
Non-POU domain-containing octamer-binding protein (53-312) monomer, 30 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 7.5, 250 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Apr 28
Structural plasticity of the coiled-coil interactions in human SFPQ. Nucleic Acids Res (2024)
Koning HJ, Lai JY, Marshall AC, Stroeher E, Monahan G, Pullakhandam A, Knott GJ, Ryan TM, Fox AH, Whitten A, Lee M, Bond CS
RgGuinier 3.0 nm
Dmax 12.7 nm
VolumePorod 102 nm3