Browse by ORGANISM: Homo sapiens (Human)

SASDHN5 – Apolipoprotein-D plus sphingomyelin

Apolipoprotein D experimental SAS data
Apolipoprotein D Kratky plot
Sample: Apolipoprotein D tetramer, 77 kDa Homo sapiens protein
Buffer: 50 mM Na Phosphate, 150 mM NaCl, 3% glycerol, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2016 Nov 11
Small angle X-ray scattering analysis of ligand-bound forms of tetrameric apolipoprotein-D Bioscience Reports 41(1) (2021)
Kielkopf C, Whitten A, Garner B, Brown S
RgGuinier 3.3 nm
Dmax 9.9 nm
VolumePorod 171 nm3

SASDJC5 – LINC complex between the SUN domain of SUN1 and KASH domain of Nesprin-4 - SUN1-KASH4 6:6 complex

SUN domain-containing protein 1Nesprin-4 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: SUN domain-containing protein 1 hexamer, 135 kDa Homo sapiens protein
Nesprin-4 hexamer, 20 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8.0, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 May 21
A molecular mechanism for LINC complex branching by structurally diverse SUN-KASH 6:6 assemblies. Elife 10 (2021)
Gurusaran M, Davies OR
RgGuinier 4.0 nm
Dmax 13.5 nm
VolumePorod 240 nm3

SASDJD5 – LINC complex between the SUN domain of SUN1 and KASH domain of KASH5 - SUN1-KASH5 6:6 complex

SUN domain-containing protein 1Protein KASH5 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: SUN domain-containing protein 1 hexamer, 135 kDa Homo sapiens protein
Protein KASH5 hexamer, 20 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8.0, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Dec 17
A molecular mechanism for LINC complex branching by structurally diverse SUN-KASH 6:6 assemblies. Elife 10 (2021)
Gurusaran M, Davies OR
RgGuinier 3.8 nm
Dmax 13.5 nm
VolumePorod 244 nm3

SASDJE5 – LINC complex between the SUN domain of SUN1 and KASH domain of Nesprin-1 - SUN1-KASH1 6:6 complex

SUN domain-containing protein 1Nesprin-1 experimental SAS data
CORAL model
Sample: SUN domain-containing protein 1 hexamer, 135 kDa Homo sapiens protein
Nesprin-1 hexamer, 22 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8.0, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Dec 17
A molecular mechanism for LINC complex branching by structurally diverse SUN-KASH 6:6 assemblies. Elife 10 (2021)
Gurusaran M, Davies OR
RgGuinier 3.9 nm
Dmax 13.0 nm
VolumePorod 254 nm3

SASDJF5 – SUN domain of SUN1 harbouring mutation I673E - monomer

SUN domain-containing protein 1, I673E experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: SUN domain-containing protein 1, I673E monomer, 23 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8.0, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Jul 29
A molecular mechanism for LINC complex branching by structurally diverse SUN-KASH 6:6 assemblies. Elife 10 (2021)
Gurusaran M, Davies OR
RgGuinier 2.1 nm
Dmax 8.2 nm
VolumePorod 42 nm3

SASDJ52 – DNA repair protein XRCC1ΔN monomer/dimer

DNA repair protein XRCC1ΔN experimental SAS data
BILBOMD model
Sample: DNA repair protein XRCC1ΔN dimer, 76 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl pH 7.5, 150 mM NaCl, 10% glycerol, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2011 Jul 15
An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase IIIα within a flexible DNA repair complex. Nucleic Acids Res (2020)
Hammel M, Rashid I, Sverzhinsky A, Pourfarjam Y, Tsai MS, Ellenberger T, Pascal JM, Kim IK, Tainer JA, Tomkinson AE
RgGuinier 5.4 nm
Dmax 19.5 nm
VolumePorod 170 nm3

SASDJ62 – DNA repair protein XRCC1 monomer /dimer

DNA repair protein XRCC1 experimental SAS data
BILBOMD model
Sample: DNA repair protein XRCC1, 69 kDa Homo sapiens protein
Buffer: 200 mM NaCl, 20 mM Tris-HCl, pH 7.5, 2% glycerol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 19
An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase IIIα within a flexible DNA repair complex. Nucleic Acids Res (2020)
Hammel M, Rashid I, Sverzhinsky A, Pourfarjam Y, Tsai MS, Ellenberger T, Pascal JM, Kim IK, Tainer JA, Tomkinson AE
RgGuinier 6.3 nm
Dmax 26.9 nm
VolumePorod 330 nm3

SASDJ72 – DNA Ligase IIIα monomer/dimer

DNA ligase 3 (DNA ligase III alpha) experimental SAS data
BILBOMD model
Sample: DNA ligase 3 (DNA ligase III alpha), Homo sapiens protein
Buffer: 25 mM Tris-HCl pH 7.5, 150 mM NaCl, 10% glycerol, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2011 Mar 31
An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase IIIα within a flexible DNA repair complex. Nucleic Acids Res (2020)
Hammel M, Rashid I, Sverzhinsky A, Pourfarjam Y, Tsai MS, Ellenberger T, Pascal JM, Kim IK, Tainer JA, Tomkinson AE
RgGuinier 6.1 nm
Dmax 21.0 nm
VolumePorod 240 nm3

SASDJ82 – DNA repair protein XRCC1 - DNA Ligase IIIα complex

DNA repair protein XRCC1DNA ligase 3 (DNA ligase III alpha) experimental SAS data
BILBOMD model
Sample: DNA repair protein XRCC1, 69 kDa Homo sapiens protein
DNA ligase 3 (DNA ligase III alpha), Homo sapiens protein
Buffer: 50 mM Tris-HCl, pH 7.5, 100 mM NaCl, 5 mM MgCl₂,  0.2 mM PMSF, 1 mM benzamidine, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Aug 18
An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase IIIα within a flexible DNA repair complex. Nucleic Acids Res (2020)
Hammel M, Rashid I, Sverzhinsky A, Pourfarjam Y, Tsai MS, Ellenberger T, Pascal JM, Kim IK, Tainer JA, Tomkinson AE
RgGuinier 6.2 nm
Dmax 27.9 nm
VolumePorod 675 nm3

SASDHU4 – ECSIT C-terminal domain

Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial experimental SAS data
DAMMIN model
Sample: Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial dimer, 44 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 250 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Dec 7
Assembly of the mitochondrial Complex I assembly complex suggests a regulatory role for deflavination. Angew Chem Int Ed Engl (2020)
Giachin G, Jessop M, Bouverot R, Acajjaoui S, Saidi M, Chretien A, Bacia-Verloop M, Signor L, Mas PJ, Favier A, Borel Meneroud E, Hons M, Hart DJ, Kandiah E, Boeri Erba E, Buisson A, Leonard G, Gutsche I, Soler-Lopez M
RgGuinier 3.7 nm
Dmax 11.9 nm
VolumePorod 117 nm3