Small Angle Scattering Biological Data Bank SASBDB


Advanced search

9 hits found for Koning

SASDNV2 – The pro-convertase formed by human FB and cobra venom factor (CVF)

Cobra venom factor experimental SAS data

Sample:	Cobra venom factor monomer, 185 kDa Naja kaouthia protein
Buffer:	10 mM Tris 5 mM MgCl2 10 mM NaCl, pH: 7.4
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Dec 19

Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex The EMBO Journal 28(16):2469-2478 (2009)
...Koning R, Svergun D, Koster A, Fritzinger D, Vogel C, Gros P

R_g^Guinier	4.6	nm
D_max	15.0	nm
Volume^Porod	384	nm³

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

Structural dynamics of IDR interactions in human SFPQ and implications for liquid–liquid phase separation Acta Crystallographica Section D Structural Biology 81(7):357-379 (2025)
Koning H, Lai V, Sethi A, Chakraborty S, Ang C, Fox A, Duff A, Whitten A, Marshall A, Bond C

R_g^Guinier	8.7	nm
D_max	30.7	nm
Volume^Porod	241000	nm³

SASDV57 – Full-length SFPQ in high salt buffer

Sample:	Splicing factor, proline- and glutamine-rich dimer, 153 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 2022 Oct 22

R_g^Guinier	7.9	nm
D_max	42.5	nm
Volume^Porod	485	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

R_g^Guinier	7.6	nm
D_max	34.3	nm
Volume^Porod	400	nm³

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

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

R_g^Guinier	6.1	nm
D_max	28.0	nm
Volume^Porod	315	nm³

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

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

R_g^Guinier	6.1	nm
D_max	22.0	nm
Volume^Porod	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

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

R_g^Guinier	5.5	nm
D_max	20.4	nm
Volume^Porod	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

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

R_g^Guinier	5.2	nm
D_max	21.0	nm
Volume^Porod	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

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

R_g^Guinier	3.0	nm
D_max	12.7	nm
Volume^Porod	102	nm³

Search