SASBDB entries for UniProt ID: P01023

SASDJK3 – Native alpha-2-macroglobulin, glycosylated

UniProt ID: P01023 (24-1474) Alpha-2-macroglobulin
Alpha-2-macroglobulin experimental SAS data
OTHER model
Sample: Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2020 Jan 22
Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Mol Cell Proteomics 20:100090 (2021)
Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ
RgGuinier 7.7 nm
Dmax 22.7 nm

SASDJL3 – Methylamine-treated alpha-2-macroglobulin, glycosylated

UniProt ID: P01023 (24-1474) Alpha-2-macroglobulin
Alpha-2-macroglobulin experimental SAS data
CUSTOM IN-HOUSE model
Sample: Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2020 Jan 22
Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Mol Cell Proteomics 20:100090 (2021)
Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ
RgGuinier 6.7 nm
Dmax 19.7 nm

SASDJM3 – Trypsin-treated alpha-2-macroglobulin, glycosylated

UniProt ID: P00760 (1-246) Cationic trypsin

UniProt ID: P01023 (24-1474) Alpha-2-macroglobulin
Cationic trypsinAlpha-2-macroglobulin experimental SAS data
CUSTOM IN-HOUSE model
Sample: Cationic trypsin dimer, 52 kDa Bos taurus protein
Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2020 Jan 15
Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Mol Cell Proteomics 20:100090 (2021)
Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ
RgGuinier 6.6 nm
Dmax 19.7 nm

SASDJN3 – Native alpha-2-macroglobulin, deglycosylated

UniProt ID: P01023 (24-1474) Alpha-2-macroglobulin
Alpha-2-macroglobulin experimental SAS data
CUSTOM IN-HOUSE model
Sample: Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2019 Apr 12
Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Mol Cell Proteomics 20:100090 (2021)
Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ
RgGuinier 7.6 nm
Dmax 20.2 nm

SASDJP3 – Methylamine-treated alpha-2-macroglobulin, deglcycosylated

UniProt ID: P01023 (24-1474) Alpha-2-macroglobulin
Alpha-2-macroglobulin experimental SAS data
CUSTOM IN-HOUSE model
Sample: Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2019 Apr 13
Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Mol Cell Proteomics 20:100090 (2021)
Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ
RgGuinier 6.6 nm
Dmax 19.7 nm

SASDJQ3 – Trypsin-treated alpha-2-macroglobulin, deglycosylated

UniProt ID: P00760 (1-246) Cationic trypsin

UniProt ID: P01023 (24-1474) Alpha-2-macroglobulin
Cationic trypsinAlpha-2-macroglobulin experimental SAS data
CUSTOM IN-HOUSE model
Sample: Cationic trypsin dimer, 52 kDa Bos taurus protein
Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2020 Jan 22
Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism. Mol Cell Proteomics 20:100090 (2021)
Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ
RgGuinier 6.6 nm
Dmax 20.7 nm