Browse by MACROMOLECULE type: protein

SASDEF4 – Tryparedoxin K102E, reduced state

Tryparedoxin K102E experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Tryparedoxin K102E monomer, 16 kDa Trypanosoma brucei brucei protein
Buffer: 10 mM HEPES pH 7.5, 50 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 May 31
Inhibitor-induced dimerization of an essential oxidoreductase from African Trypanosomes. Angew Chem Int Ed Engl (2019)
Wagner A, Le TA, Brennich M, Klein P, Bader N, Diehl E, Paszek D, Weickhmann AK, Dirdjaja N, Krauth-Siegel RL, Engels B, Opatz T, Schindelin H, Hellmich UA
RgGuinier 1.6 nm
Dmax 6.0 nm
VolumePorod 29 nm3

SASDEG4 – Tryparedoxin K102E, oxidized state

Tryparedoxin K102E experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Tryparedoxin K102E monomer, 16 kDa Trypanosoma brucei brucei protein
Buffer: 10 mM HEPES pH 7.5, 50 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 May 31
Inhibitor-induced dimerization of an essential oxidoreductase from African Trypanosomes. Angew Chem Int Ed Engl (2019)
Wagner A, Le TA, Brennich M, Klein P, Bader N, Diehl E, Paszek D, Weickhmann AK, Dirdjaja N, Krauth-Siegel RL, Engels B, Opatz T, Schindelin H, Hellmich UA
RgGuinier 1.6 nm
Dmax 4.3 nm
VolumePorod 26 nm3

SASDEH4 – Tryparedoxin K102E, in the presence of inhibitor CFT (2-(chloromethyl)-5-(4-fluorophenyl)thieno[2,3-d]pyrimidin-4(3H)-one)

Tryparedoxin K102E experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Tryparedoxin K102E, 16 kDa Trypanosoma brucei brucei protein
Buffer: 10 mM HEPES pH 7.5, 50 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 May 31
Inhibitor-induced dimerization of an essential oxidoreductase from African Trypanosomes. Angew Chem Int Ed Engl (2019)
Wagner A, Le TA, Brennich M, Klein P, Bader N, Diehl E, Paszek D, Weickhmann AK, Dirdjaja N, Krauth-Siegel RL, Engels B, Opatz T, Schindelin H, Hellmich UA
RgGuinier 1.8 nm
Dmax 6.2 nm
VolumePorod 37 nm3

SASDFJ3 – Maltose binding protein-SpoIVB peptidase fusion (MBP-SpoIVB)

SpoIVB peptidase (MBP fusion) experimental SAS data
CHIMERA model
Sample: SpoIVB peptidase (MBP fusion) monomer, 80 kDa Bacillus subtilis protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, 5% glycerol, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2018 Jul 12
Solution Structure of SpoIVB Reveals Mechanism of PDZ Domain-Regulated Protease Activity. Front Microbiol 10:1232 (2019)
Xie X, Guo N, Xue G, Xie D, Yuan C, Harrison J, Li J, Jiang L, Huang M
RgGuinier 3.7 nm
Dmax 15.6 nm
VolumePorod 96 nm3

SASDFV8 – Apolipoprotein E2 (ApoE2) bound to 4 µg/mL heparin

Apolipoprotein E2Heparin experimental SAS data
Apolipoprotein E2 Heparin Kratky plot
Sample: Apolipoprotein E2 tetramer, 139 kDa Homo sapiens protein
Heparin monomer, 15 kDa
Buffer: 20 mM HEPES, 300 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 May 3
Therapeutic approaches to ApoE University of Sussex PhD thesis 2019 (2019)
Lucas Kraft
RgGuinier 6.2 nm
Dmax 20.7 nm
VolumePorod 504 nm3

SASDFW8 – Apolipoprotein E2 (ApoE2) bound to 12 µg/mL heparin

Apolipoprotein E2Heparin experimental SAS data
Apolipoprotein E2 Heparin Kratky plot
Sample: Apolipoprotein E2 tetramer, 139 kDa Homo sapiens protein
Heparin monomer, 15 kDa
Buffer: 20 mM HEPES, 300 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 May 3
Therapeutic approaches to ApoE University of Sussex PhD thesis 2019 (2019)
Lucas Kraft
RgGuinier 6.4 nm
Dmax 21.7 nm
VolumePorod 531 nm3

SASDFX8 – Apolipoprotein E2 (ApoE2) bound to 37 µg/mL heparin

Apolipoprotein E2Heparin experimental SAS data
Apolipoprotein E2 Heparin Kratky plot
Sample: Apolipoprotein E2 tetramer, 139 kDa Homo sapiens protein
Heparin monomer, 15 kDa
Buffer: 20 mM HEPES, 300 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 May 3
Therapeutic approaches to ApoE University of Sussex PhD thesis 2019 (2019)
Lucas Kraft
RgGuinier 6.5 nm
Dmax 23.4 nm
VolumePorod 584 nm3

SASDFY8 – Apolipoprotein E2 (ApoE2) bound to 110 µg/mL heparin

Apolipoprotein E2Heparin experimental SAS data
Apolipoprotein E2 Heparin Kratky plot
Sample: Apolipoprotein E2 tetramer, 139 kDa Homo sapiens protein
Heparin monomer, 15 kDa
Buffer: 20 mM HEPES, 300 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 May 3
Therapeutic approaches to ApoE University of Sussex PhD thesis 2019 (2019)
Lucas Kraft
RgGuinier 7.1 nm
Dmax 24.0 nm
VolumePorod 666 nm3

SASDFZ8 – Apolipoprotein E2 (ApoE2) bound to 330 µg/mL heparin

Apolipoprotein E2Heparin experimental SAS data
Apolipoprotein E2 Heparin Kratky plot
Sample: Apolipoprotein E2 tetramer, 139 kDa Homo sapiens protein
Heparin monomer, 15 kDa
Buffer: 20 mM HEPES, 300 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 May 3
Therapeutic approaches to ApoE University of Sussex PhD thesis 2019 (2019)
Lucas Kraft
RgGuinier 7.2 nm
Dmax 24.5 nm
VolumePorod 696 nm3

SASDG25 – DNA repair protein Rad5 (with 6xhis and twin-strep tags)

DNA repair protein RAD5 experimental SAS data
OTHER [STATIC IMAGE] model
Sample: DNA repair protein RAD5 monomer, 138 kDa Saccharomyces cerevisiae protein
Buffer: 40 mM Tris, 150 mM KCl, 5 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Mar 6
Conformational flexibility of fork-remodeling helicase Rad5 shown by full-ensemble hybrid methods. PLoS One 14(10):e0223875 (2019)
Gildenberg MS, Washington MT
RgGuinier 4.7 nm
Dmax 17.8 nm
VolumePorod 254 nm3