Browse by MACROMOLECULE type: protein

SASDB36 – Glycosylated myelin-associated glycoprotein full extracellular domain (Ig1-5) N406Q mutant

Myelin-associated glycoprotein (20-508; N406Q mutant) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Myelin-associated glycoprotein (20-508; N406Q mutant) monomer, 54 kDa Mus musculus protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Feb 5
Structural basis of myelin-associated glycoprotein adhesion and signalling. Nat Commun 7:13584 (2016)
Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ
RgGuinier 7.3 nm
Dmax 25.6 nm
VolumePorod 193 nm3

SASDB46 – Glycosylated Myelin-associated glycoprotein immunoglobulin domains 1-3

Myelin-associated glycoprotein Ig domains 1-3 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Myelin-associated glycoprotein Ig domains 1-3 monomer, 35 kDa Mus musculus protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 11
Structural basis of myelin-associated glycoprotein adhesion and signalling. Nat Commun 7:13584 (2016)
Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ
RgGuinier 3.9 nm
Dmax 13.0 nm
VolumePorod 59 nm3

SASDB56 – Deglycosylated myelin-associated glycoprotein full extracellular domain (Ig 1-5) I473E mutant

Myelin-associated glycoprotein (20-508; I473E mutant) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Myelin-associated glycoprotein (20-508; I473E mutant) monomer, 54 kDa Mus musculus protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 11
Structural basis of myelin-associated glycoprotein adhesion and signalling. Nat Commun 7:13584 (2016)
Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ
RgGuinier 6.0 nm
Dmax 21.2 nm
VolumePorod 100 nm3

SASDB66 – Deglycosylated myelin-associated glycoprotein full extracellular domain (Ig 1-5) N406Q mutant

Myelin-associated glycoprotein (20-508; N406Q mutant) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Myelin-associated glycoprotein (20-508; N406Q mutant) monomer, 54 kDa Mus musculus protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2015 Jul 28
Structural basis of myelin-associated glycoprotein adhesion and signalling. Nat Commun 7:13584 (2016)
Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ
RgGuinier 7.8 nm
Dmax 29.0 nm
VolumePorod 216 nm3

SASDB76 – Deglycosylated myelin-associated glycoprotein (immunoglobulin domains 1-3)

Myelin-associated glycoprotein Ig domains 1-3 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Myelin-associated glycoprotein Ig domains 1-3 monomer, 35 kDa Mus musculus protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 11
Structural basis of myelin-associated glycoprotein adhesion and signalling. Nat Commun 7:13584 (2016)
Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ
RgGuinier 3.9 nm
Dmax 12.6 nm
VolumePorod 49 nm3

SASDBF6 – Deglycosylated myelin-associated glycoprotein full extracellular domain (immunoglobulin domains 1-5)

Myelin-associated glycoprotein Ig domains 1-5 experimental SAS data
NONE model
Sample: Myelin-associated glycoprotein Ig domains 1-5 dimer, 108 kDa Mus musculus protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 11
Structural basis of myelin-associated glycoprotein adhesion and signalling. Nat Commun 7:13584 (2016)
Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ
RgGuinier 7.3 nm
Dmax 25.5 nm
VolumePorod 166 nm3

SASDBA5 – Cyclohexanone monooxygenase, wild-type

Cyclohexanone monooxygenase experimental SAS data
Cyclohexanone monooxygenase Kratky plot
Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein
Buffer: 50 mM Tris, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 2
The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure. Biochim Biophys Acta 1864(12):1641-1648 (2016)
Yachnin BJ, Lau PCK, Berghuis AM
RgGuinier 2.7 nm
Dmax 9.3 nm
VolumePorod 110 nm3

SASDBB5 – Cyclohexanone monooxygenase, NADP+, wild-type

Cyclohexanone monooxygenase experimental SAS data
Cyclohexanone monooxygenase Kratky plot
Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein
Buffer: 50 mM Tris 5 mM NADP+, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2013 Jan 27
The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure. Biochim Biophys Acta 1864(12):1641-1648 (2016)
Yachnin BJ, Lau PCK, Berghuis AM
RgGuinier 2.6 nm
Dmax 8.0 nm
VolumePorod 99 nm3

SASDBC5 – Cyclohexanone monooxygenase, NADP+ and cyclohexanone, wild-type

Cyclohexanone monooxygenase experimental SAS data
Cyclohexanone monooxygenase Kratky plot
Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein
Buffer: 50 mM Tris 5 mM NADP+ 5 mM cyclohexanone, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 2
The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure. Biochim Biophys Acta 1864(12):1641-1648 (2016)
Yachnin BJ, Lau PCK, Berghuis AM
RgGuinier 2.5 nm
Dmax 7.8 nm
VolumePorod 100 nm3

SASDBD5 – Cyclohexanone monooxygenase, NADP+ and ε-caprolactone, wild-type

Cyclohexanone monooxygenase experimental SAS data
Cyclohexanone monooxygenase Kratky plot
Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein
Buffer: 50 mM Tris 5 mM NADP+ 5 mM ε-caprolactone, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 2
The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure. Biochim Biophys Acta 1864(12):1641-1648 (2016)
Yachnin BJ, Lau PCK, Berghuis AM
RgGuinier 2.5 nm
Dmax 7.5 nm
VolumePorod 99 nm3