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7 hits found for Jan Skov Pedersen

SASDJK3 – Native alpha-2-macroglobulin, glycosylated

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 ...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)
...Pedersen JS, Enghild JJ
RgGuinier 7.7 nm
Dmax 22.7 nm

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

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 ...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)
...Pedersen JS, Enghild JJ
RgGuinier 6.7 nm
Dmax 19.7 nm

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

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 ...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)
...Pedersen JS, Enghild JJ
RgGuinier 6.6 nm
Dmax 19.7 nm

SASDJN3 – Native alpha-2-macroglobulin, deglycosylated

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)
...Pedersen JS, Enghild JJ
RgGuinier 7.6 nm
Dmax 20.2 nm

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

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)
...Pedersen JS, Enghild JJ
RgGuinier 6.6 nm
Dmax 19.7 nm

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

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 ...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)
...Pedersen JS, Enghild JJ
RgGuinier 6.6 nm
Dmax 20.7 nm

SASDXF6 – Multi-domain human O-GlcNAcase

Protein O-GlcNAcase experimental SAS data
ALPHAFOLD model
Sample: Protein O-GlcNAcase dimer, 163 kDa Homo sapiens protein
Buffer: 25 mM Tris buffer, 150 mM NaCl, and 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2023 Jun 22
Multi-domain O-GlcNAcase structures reveal allosteric regulatory mechanisms
Jan Skov Pedersen
RgGuinier 5.4 nm
Dmax 18.9 nm
VolumePorod 443 nm3