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31 hits found for 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 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)
...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 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)
...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 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)
...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 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)
...Pedersen JS, Enghild JJ
RgGuinier 6.6 nm
Dmax 20.7 nm

SASDKA4 – Complement factor P, properdin (FP) dimer

Properdin (dimer) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Properdin (dimer) dimer, 110 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Nov 14
Properdin oligomers adopt rigid extended conformations supporting function. Elife 10 (2021)
Pedersen DV, Pedersen MN, Mazarakis SM, Wang Y, Lindorff-Larsen K, Arleth L, Andersen GR
RgGuinier 8.1 nm
Dmax 24.0 nm

SASDKB4 – Complement factor P, properdin (FP) trimer

Properdin (trimer) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Properdin (trimer) trimer, 165 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Nov 14
Properdin oligomers adopt rigid extended conformations supporting function. Elife 10 (2021)
Pedersen DV, Pedersen MN, Mazarakis SM, Wang Y, Lindorff-Larsen K, Arleth L, Andersen GR
RgGuinier 10.2 nm
Dmax 27.0 nm

SASDKC4 – Complement factor P, properdin (FP) tetramer

Properdin (tetramer) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Properdin (tetramer) tetramer, 220 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Nov 14
Properdin oligomers adopt rigid extended conformations supporting function. Elife 10 (2021)
Pedersen DV, Pedersen MN, Mazarakis SM, Wang Y, Lindorff-Larsen K, Arleth L, Andersen GR
RgGuinier 13.1 nm
Dmax 36.0 nm

SASDEY4 – Ribonuclease A monomer from in-house SEC-SAXS

Ribonuclease pancreatic experimental SAS data
PDB model
Sample: Ribonuclease pancreatic monomer, 14 kDa Bos taurus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2018 Jan 23
Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument. J Appl Crystallogr 51(Pt 6):1623-1632 (2018)
...Pedersen M, Skou S, Arleth L, Vestergaard B
RgGuinier 1.5 nm
Dmax 4.8 nm
VolumePorod 10 nm3

SASDEZ4 – Carbonic Anhydrase from in-house SEC-SAXS

Carbonic anhydrase 2 experimental SAS data
PDB model
Sample: Carbonic anhydrase 2 monomer, 29 kDa Bos taurus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2018 Jan 24
Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument. J Appl Crystallogr 51(Pt 6):1623-1632 (2018)
...Pedersen M, Skou S, Arleth L, Vestergaard B
RgGuinier 1.9 nm
Dmax 5.3 nm
VolumePorod 38 nm3

SASDE25 – Human insulin hexamer from in-house SEC-SAXS

Human insulin experimental SAS data
DAMFILT model
Sample: Human insulin hexamer, 35 kDa Homo sapiens protein
Buffer: 7 mM sodium phosphate, 60 mM phenol, 200 µM Zn(CH3COO)2, 23 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2018 Jan 26
Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument. J Appl Crystallogr 51(Pt 6):1623-1632 (2018)
...Pedersen M, Skou S, Arleth L, Vestergaard B
RgGuinier 2.0 nm
Dmax 5.9 nm
VolumePorod 39 nm3

SASDE35 – Ovalbumin monomer from in-house SEC-SAXS

Ovalbumin experimental SAS data
PDB model
Sample: Ovalbumin monomer, 43 kDa Gallus gallus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2018 Jan 24
Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument. J Appl Crystallogr 51(Pt 6):1623-1632 (2018)
...Pedersen M, Skou S, Arleth L, Vestergaard B
RgGuinier 2.4 nm
Dmax 7.8 nm
VolumePorod 55 nm3

SASDE45 – Conalbumin monomer from in-house SEC-SAXS

Ovotransferrin experimental SAS data
PDB model
Sample: Ovotransferrin monomer, 76 kDa Gallus gallus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2018 Jan 24
Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument. J Appl Crystallogr 51(Pt 6):1623-1632 (2018)
...Pedersen M, Skou S, Arleth L, Vestergaard B
RgGuinier 3.0 nm
Dmax 10.1 nm
VolumePorod 100 nm3

SASDE55 – Apoferritin monomer from in-house SEC-SAXS

Ferritin light chain experimental SAS data
PDB model
Sample: Ferritin light chain 24-mer, 476 kDa Equus caballus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2018 Jan 24
Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument. J Appl Crystallogr 51(Pt 6):1623-1632 (2018)
...Pedersen M, Skou S, Arleth L, Vestergaard B
RgGuinier 5.1 nm
Dmax 12.3 nm
VolumePorod 685 nm3

SASDE65 – Bovine serum albumin monomer from in-house SEC-SAXS

Bovine serum albumin experimental SAS data
PDB model
Sample: Bovine serum albumin monomer, 66 kDa Bos taurus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2018 Jan 23
Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument. J Appl Crystallogr 51(Pt 6):1623-1632 (2018)
...Pedersen M, Skou S, Arleth L, Vestergaard B
RgGuinier 2.8 nm
Dmax 9.2 nm
VolumePorod 92 nm3

SASDE75 – Bovine serum albumin monomer from in-house SEC-SAXS

Bovine serum albumin experimental SAS data
PDB model
Sample: Bovine serum albumin monomer, 66 kDa Bos taurus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2018 Jan 23
Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument. J Appl Crystallogr 51(Pt 6):1623-1632 (2018)
...Pedersen M, Skou S, Arleth L, Vestergaard B
RgGuinier 2.8 nm
Dmax 9.9 nm
VolumePorod 104 nm3

SASDE85 – Bovine serum albumin monomer from in-house SEC-SAXS

Bovine serum albumin experimental SAS data
PDB model
Sample: Bovine serum albumin monomer, 66 kDa Bos taurus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2018 Jan 23
Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument. J Appl Crystallogr 51(Pt 6):1623-1632 (2018)
...Pedersen M, Skou S, Arleth L, Vestergaard B
RgGuinier 2.8 nm
Dmax 8.2 nm
VolumePorod 85 nm3

SASDE95 – Bovine serum albumin monomer from in-house SEC-SAXS

Bovine serum albumin experimental SAS data
PDB model
Sample: Bovine serum albumin monomer, 66 kDa Bos taurus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2018 Jan 23
Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument. J Appl Crystallogr 51(Pt 6):1623-1632 (2018)
...Pedersen M, Skou S, Arleth L, Vestergaard B
RgGuinier 2.9 nm
Dmax 8.6 nm
VolumePorod 74 nm3

SASDEA5 – Bovine serum albumin monomer from in-house SEC-SAXS

Bovine serum albumin experimental SAS data
PDB model
Sample: Bovine serum albumin monomer, 66 kDa Bos taurus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2018 Jan 25
Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument. J Appl Crystallogr 51(Pt 6):1623-1632 (2018)
...Pedersen M, Skou S, Arleth L, Vestergaard B
RgGuinier 2.8 nm
Dmax 9.6 nm
VolumePorod 78 nm3

SASDEB5 – Bovine serum albumin from in-house SAXS

Bovine serum albumin experimental SAS data
PDB model
Sample: Bovine serum albumin monomer, 66 kDa Bos taurus protein
Buffer: 50 mM HEPES, pH: 7.5
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2018 May 4
Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument. J Appl Crystallogr 51(Pt 6):1623-1632 (2018)
...Pedersen M, Skou S, Arleth L, Vestergaard B
RgGuinier 2.8 nm
Dmax 9.4 nm
VolumePorod 99 nm3

SASDEC5 – Bovine serum albumin dimer from in-house SEC-SAXS

Bovine serum albumin experimental SAS data
PDB model
Sample: Bovine serum albumin dimer, 133 kDa Bos taurus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, University of Copenhagen, Department of Drug Design and Pharmacology on 2018 Jan 23
Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument. J Appl Crystallogr 51(Pt 6):1623-1632 (2018)
...Pedersen M, Skou S, Arleth L, Vestergaard B
RgGuinier 4.1 nm
Dmax 13.8 nm
VolumePorod 200 nm3

SASDED5 – Bovine serum albumin monomer from synchrotron SEC-SAXS

Bovine serum albumin experimental SAS data
PDB model
Sample: Bovine serum albumin monomer, 66 kDa Bos taurus protein
Buffer: PBS + 1 mM DTT, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Jun 14
Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument. J Appl Crystallogr 51(Pt 6):1623-1632 (2018)
...Pedersen M, Skou S, Arleth L, Vestergaard B
RgGuinier 2.7 nm
Dmax 8.7 nm
VolumePorod 84 nm3

SASDEE5 – Bovine serum albumin from synchrotron SAXS

Bovine serum albumin experimental SAS data
PDB model
Sample: Bovine serum albumin monomer, 66 kDa Bos taurus protein
Buffer: 50 mM HEPES, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Nov 26
Size-exclusion chromatography small-angle X-ray scattering of water soluble proteins on a laboratory instrument. J Appl Crystallogr 51(Pt 6):1623-1632 (2018)
...Pedersen M, Skou S, Arleth L, Vestergaard B
RgGuinier 2.8 nm
Dmax 9.5 nm
VolumePorod 85 nm3

SASDBZ7 – Complement factor 1s in complex with Complement factor 1r

Complement C1r subcomponentComplement C1s subcomponent experimental SAS data
CORAL model
Sample: Complement C1r subcomponent dimer, 156 kDa Homo sapiens protein
Complement C1s subcomponent dimer, 150 kDa Homo sapiens protein
Buffer: 50 mM TrisHCl, 145 mM NaCl, 3 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2014 Dec 8
Structure and activation of C1, the complex initiating the classical pathway of the complement cascade. Proc Natl Acad Sci U S A 114(5):986-991 (2017)
...Pedersen JS, Golas MM, Jensenius JC, Hansen AG, Thiel S, Andersen GR
RgGuinier 11.6 nm

SASDB28 – Complement factor 1q (C1q)

Complement C1q subcomponent subunit CComplement C1q subcomponent subunit BComplement C1q subcomponent subunit A experimental SAS data
Complement C1q subcomponent subunit C Complement C1q subcomponent subunit B Complement C1q subcomponent subunit A Kratky plot
Sample: Complement C1q subcomponent subunit C hexamer, 142 kDa Homo sapiens protein
Complement C1q subcomponent subunit B hexamer, 142 kDa Homo sapiens protein
Complement C1q subcomponent subunit A hexamer, 142 kDa Homo sapiens protein
Buffer: 50 mM TrisHCl, 145 mM NaCl, 3 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2014 Dec 8
Structure and activation of C1, the complex initiating the classical pathway of the complement cascade. Proc Natl Acad Sci U S A 114(5):986-991 (2017)
...Pedersen JS, Golas MM, Jensenius JC, Hansen AG, Thiel S, Andersen GR
RgGuinier 12.6 nm

SASDB38 – Inactivated complement factor 1 (C1)

Complement C1q subcomponent subunit CComplement C1q subcomponent subunit BComplement C1q subcomponent subunit AComplement C1r subcomponentComplement C1s subcomponent experimental SAS data
CORAL model
Sample: Complement C1q subcomponent subunit C hexamer, 142 kDa Homo sapiens protein
Complement C1q subcomponent subunit B hexamer, 142 kDa Homo sapiens protein
Complement C1q subcomponent subunit A hexamer, 142 kDa Homo sapiens protein
Complement C1r subcomponent dimer, 156 kDa Homo sapiens protein
Complement C1s subcomponent dimer, 150 kDa Homo sapiens protein
Buffer: 50 mM EPPS, 145 mM NaCl, 3 mM CaCl2, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Aug 16
Structure and activation of C1, the complex initiating the classical pathway of the complement cascade. Proc Natl Acad Sci U S A 114(5):986-991 (2017)
...Pedersen JS, Golas MM, Jensenius JC, Hansen AG, Thiel S, Andersen GR
RgGuinier 11.5 nm
Dmax 36.6 nm

SASDB59 – Recombinant monomeric human Properdin

Human recombinant Properdin TSR 0-3Human recombinant Properdin TSR 4-6 experimental SAS data
CORAL model
Sample: Human recombinant Properdin TSR 0-3 monomer, 25 kDa Homo sapiens protein
Human recombinant Properdin TSR 4-6 monomer, 24 kDa Homo sapiens protein
Buffer: 10 mM HEPES 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Aug 16
Functional and structural insight into properdin control of complement alternative pathway amplification. EMBO J 36(8):1084-1099 (2017)
Pedersen DV, Roumenina L, Jensen RK, Gadeberg TA, Marinozzi C, Picard C, Rybkine T, Thiel S, Sørensen UB, Stover C, Fremeaux-Bacchi V, Andersen GR
RgGuinier 5.1 nm
Dmax 18.0 nm

SASDB69 – E244K monomeric human Properdin

E244K Human Properdin experimental SAS data
CORAL model
Sample: E244K Human Properdin monomer, 49 kDa Homo sapiens protein
Buffer: 10 mM HEPES 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Jul 27
Functional and structural insight into properdin control of complement alternative pathway amplification. EMBO J 36(8):1084-1099 (2017)
Pedersen DV, Roumenina L, Jensen RK, Gadeberg TA, Marinozzi C, Picard C, Rybkine T, Thiel S, Sørensen UB, Stover C, Fremeaux-Bacchi V, Andersen GR
RgGuinier 4.1 nm
Dmax 15.0 nm

SASDEL9 – Escherichia coli aerobic fatty acid beta-oxidation trifunctional enzyme complex

Fatty acid oxidation complex subunit alphaFatty acid oxidation complex subunit alpha3-ketoacyl-CoA thiolase FadA (beta subunit) experimental SAS data
DAMMIN model
Sample: Fatty acid oxidation complex subunit alpha monomer, 81 kDa Escherichia coli protein
Fatty acid oxidation complex subunit alpha monomer, 81 kDa Escherichia coli protein
3-ketoacyl-CoA thiolase FadA (beta subunit) dimer, 82 kDa Escherichia coli protein
Buffer: 20 mM 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES), 120 mM KCl, 2.5 mM DTT, pH: 7.2
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 May 30
Complementary substrate specificity and distinct quaternary assembly of the Escherichia coli aerobic and anaerobic beta-oxidation trifunctional enzyme complexes. Biochem J (2019)
...Pedersen JS, Butcher SJ, Wierenga RK, Venkatesan R
RgGuinier 4.6 nm
Dmax 16.0 nm
VolumePorod 406 nm3

SASDEM9 – anEcTFE: Escherichia coli anaerobic fatty acid beta-oxidation trifunctional enzyme complex

Fatty acid oxidation complex subunit alphaanaerobic Fatty acid oxidation complex subunit alphaanaerobic Fatty acid oxidation complex subunit alphaanaerobic Fatty acid oxidation complex subunit alphaanaerobic 3-ketoacyl-CoA thiolase FadI beta subunitanaerobic 3-ketoacyl-CoA thiolase FadI beta subunit experimental SAS data
DAMMIN model
Sample: Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli (strain … protein
anaerobic Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli protein
anaerobic Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli protein
anaerobic Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli protein
anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit dimer, 96 kDa Escherichia coli protein
anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit dimer, 96 kDa Escherichia coli protein
Buffer: 50 mM Tris, 500 mM NaCl, 5% glycerol, 0.05% C12E9 (1-O-(n-Dodecyl)-nonaethyleneglycol), 2.5 mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2015 Sep 22
Complementary substrate specificity and distinct quaternary assembly of the Escherichia coli aerobic and anaerobic beta-oxidation trifunctional enzyme complexes. Biochem J (2019)
...Pedersen JS, Butcher SJ, Wierenga RK, Venkatesan R
RgGuinier 6.2 nm
Dmax 19.6 nm
VolumePorod 856 nm3