Browse by ORGANISM: Homo sapiens (Human)

SASDJP9 – Saposin-A plus LMNG (2,2-didecylpropane-1,3-bis-β-D-maltopyranoside)

Prosaposin (Saposin-A)2,2-didecylpropane-1,3-bis-β-D-maltopyranoside experimental SAS data
Prosaposin (Saposin-A) 2,2-didecylpropane-1,3-bis-β-D-maltopyranoside Kratky plot
Sample: Prosaposin (Saposin-A) dimer, 19 kDa Homo sapiens protein
2,2-didecylpropane-1,3-bis-β-D-maltopyranoside 0, 15 kDa
Buffer: 25 mM Tris-HCl, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Feb 18
Stable Picodisc Assemblies from Saposin Proteins and Branched Detergents. Biochemistry 60(14):1108-1119 (2021)
Kurgan KW, Chen B, Brown KA, Falco Cobra P, Ye X, Ge Y, Gellman SH
RgGuinier 2.5 nm
Dmax 7.0 nm

SASDJQ9 – Saposin-B, R232W mutant

Prosaposin (Saposin-B, R232W mutant) experimental SAS data
Prosaposin (Saposin-B, R232W mutant) Kratky plot
Sample: Prosaposin (Saposin-B, R232W mutant) dimer, 18 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Feb 18
Stable Picodisc Assemblies from Saposin Proteins and Branched Detergents. Biochemistry 60(14):1108-1119 (2021)
Kurgan KW, Chen B, Brown KA, Falco Cobra P, Ye X, Ge Y, Gellman SH
RgGuinier 2.0 nm
Dmax 5.8 nm

SASDJR9 – Saposin-B, R232W mutant, plus MNA C12 (1,2,5,6-tetra-β-D-glucopyranoside-3,4-O-Di-dodecyl-d-mannitol)

1,2,5,6-tetra-β-D-glucopyranoside-3,4-O-Di-dodecyl-d-mannitolProsaposin (Saposin-B, R232W mutant) experimental SAS data
1,2,5,6-tetra-β-D-glucopyranoside-3,4-O-Di-dodecyl-d-mannitol Prosaposin (Saposin-B, R232W mutant) Kratky plot
Sample: 1,2,5,6-tetra-β-D-glucopyranoside-3,4-O-Di-dodecyl-d-mannitol decamer, 12 kDa
Prosaposin (Saposin-B, R232W mutant) dimer, 18 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Feb 18
Stable Picodisc Assemblies from Saposin Proteins and Branched Detergents. Biochemistry 60(14):1108-1119 (2021)
Kurgan KW, Chen B, Brown KA, Falco Cobra P, Ye X, Ge Y, Gellman SH
RgGuinier 2.3 nm
Dmax 6.9 nm

SASDJS9 – Saposin-B, R232W mutant, plus MNA C13 (1,2,5,6-tetra-β-D-glucopyranoside-3,4-O-Di-tridecyl-d-mannitol)

1,2,5,6-tetra-β-D-glucopyranoside-3,4-O-Di-tridecyl-d-mannitolProsaposin (Saposin-B, R232W mutant) experimental SAS data
1,2,5,6-tetra-β-D-glucopyranoside-3,4-O-Di-tridecyl-d-mannitol Prosaposin (Saposin-B, R232W mutant) Kratky plot
Sample: 1,2,5,6-tetra-β-D-glucopyranoside-3,4-O-Di-tridecyl-d-mannitol decamer, 12 kDa
Prosaposin (Saposin-B, R232W mutant) dimer, 18 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Feb 18
Stable Picodisc Assemblies from Saposin Proteins and Branched Detergents. Biochemistry 60(14):1108-1119 (2021)
Kurgan KW, Chen B, Brown KA, Falco Cobra P, Ye X, Ge Y, Gellman SH
RgGuinier 2.6 nm
Dmax 7.7 nm

SASDJT9 – Saposin-B, R232W mutant, plus LMNG (2,2-didecylpropane-1,3-bis-β-D-maltopyranoside)

2,2-didecylpropane-1,3-bis-β-D-maltopyranosideProsaposin (Saposin-B, R232W mutant) experimental SAS data
2,2-didecylpropane-1,3-bis-β-D-maltopyranoside Prosaposin (Saposin-B, R232W mutant) Kratky plot
Sample: 2,2-didecylpropane-1,3-bis-β-D-maltopyranoside 0, 15 kDa
Prosaposin (Saposin-B, R232W mutant) dimer, 18 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Feb 18
Stable Picodisc Assemblies from Saposin Proteins and Branched Detergents. Biochemistry 60(14):1108-1119 (2021)
Kurgan KW, Chen B, Brown KA, Falco Cobra P, Ye X, Ge Y, Gellman SH
RgGuinier 2.8 nm
Dmax 8.9 nm

SASDKT8 – von Willebrand Factor peptide 3mg/ml

von Willebrand factor experimental SAS data
von Willebrand factor Kratky plot
Sample: Von Willebrand factor monomer, 11 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Aug 24
An Integrative Structural Biology Analysis of Von Willebrand Factor Binding and Processing by ADAMTS-13 in Solution. J Mol Biol 433(13):166954 (2021)
Del Amo-Maestro L, Sagar A, Pompach P, Goulas T, Scavenius C, Ferrero DS, Castrillo-Briceño M, Taulés M, Enghild JJ, Bernadó P, Gomis-Rüth FX
RgGuinier 3.1 nm
Dmax 14.0 nm
VolumePorod 28 nm3

SASDKU8 – von Willebrand Factor peptide 6mg/ml

von Willebrand factor experimental SAS data
von Willebrand Factor peptide 6mg/ml Rg histogram
Sample: Von Willebrand factor monomer, 11 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Aug 24
An Integrative Structural Biology Analysis of Von Willebrand Factor Binding and Processing by ADAMTS-13 in Solution. J Mol Biol 433(13):166954 (2021)
Del Amo-Maestro L, Sagar A, Pompach P, Goulas T, Scavenius C, Ferrero DS, Castrillo-Briceño M, Taulés M, Enghild JJ, Bernadó P, Gomis-Rüth FX
RgGuinier 3.0 nm
Dmax 14.9 nm
VolumePorod 27 nm3

SASDKV8 – ADAMTS-13 bound to von Willebrand Factor peptide

von Willebrand factorA disintegrin and metalloproteinase with thrombospondin motifs 13 experimental SAS data
ADAMTS-13 bound to von Willebrand Factor peptide Rg histogram
Sample: Von Willebrand factor monomer, 11 kDa Homo sapiens protein
A disintegrin and metalloproteinase with thrombospondin motifs 13 monomer, 70 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Aug 24
An Integrative Structural Biology Analysis of Von Willebrand Factor Binding and Processing by ADAMTS-13 in Solution. J Mol Biol 433(13):166954 (2021)
Del Amo-Maestro L, Sagar A, Pompach P, Goulas T, Scavenius C, Ferrero DS, Castrillo-Briceño M, Taulés M, Enghild JJ, Bernadó P, Gomis-Rüth FX
RgGuinier 4.4 nm
Dmax 16.3 nm
VolumePorod 170 nm3

SASDFB7 – Human phenylalanine hydroxylase (hPAH)

Phenylalanine-4-hydroxylase experimental SAS data
CORAL model
Sample: Phenylalanine-4-hydroxylase tetramer, 223 kDa Homo sapiens protein
Buffer: 0.02 mM Hepes, 0.2 M NaCl,, pH: 7
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Feb 25
Modulation of Human Phenylalanine Hydroxylase by 3-Hydroxyquinolin-2(1H)-One Derivatives Biomolecules 11(3):462 (2021)
Lopes R, Tomé C, Russo R, Paterna R, Leandro J, Candeias N, Gonçalves L, Teixeira M, Sousa P, Guedes R, Vicente J, Gois P, Leandro P
RgGuinier 4.3 nm
Dmax 14.8 nm
VolumePorod 336 nm3

SASDFC7 – Human phenylalanine hydroxylase (hPAH) + 1 mM L-Phe

Phenylalanine-4-hydroxylase experimental SAS data
DAMMIN model
Sample: Phenylalanine-4-hydroxylase tetramer, 223 kDa Homo sapiens protein
Buffer: 0.02 mM Hepes, 0.2 M NaCl,, pH: 7
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Feb 25
Modulation of Human Phenylalanine Hydroxylase by 3-Hydroxyquinolin-2(1H)-One Derivatives Biomolecules 11(3):462 (2021)
Lopes R, Tomé C, Russo R, Paterna R, Leandro J, Candeias N, Gonçalves L, Teixeira M, Sousa P, Guedes R, Vicente J, Gois P, Leandro P
RgGuinier 4.0 nm
Dmax 12.3 nm
VolumePorod 367 nm3