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17 hits found for Dos Santos Morais

SASDB43 – Human dystrophin central domain repeats 1 to 2

Dystrophin central domain repeats 1 to 2 experimental SAS data
NONE model
Sample: Dystrophin central domain repeats 1 to 2 monomer, 26 kDa Homo sapiens protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2011 Oct 7
Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions. J Biol Chem 293(18):6637-6646 (2018)
...Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, ...
RgGuinier 3.0 nm
Dmax 10.6 nm
VolumePorod 42 nm3

SASDB53 – Human dystrophin central domain repeats 1 to 3

Dystrophin central domain repeats 1 to 3 experimental SAS data
NONE model
Sample: Dystrophin central domain repeats 1 to 3 monomer, 38 kDa Homo sapiens protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2011 Sep 9
Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions. J Biol Chem 293(18):6637-6646 (2018)
...Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, ...
RgGuinier 4.2 nm
Dmax 17.0 nm
VolumePorod 68 nm3

SASDB63 – Human dystrophin central domain repeats 11 to 15

Dystrophin central domain repeats 11 to 15. experimental SAS data
NONE model
Sample: Dystrophin central domain repeats 11 to 15. monomer, 60 kDa Homo sapiens protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2011 Apr 11
Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions. J Biol Chem 293(18):6637-6646 (2018)
...Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, ...
RgGuinier 5.8 nm
Dmax 23.0 nm
VolumePorod 87 nm3

SASDB73 – Human dystrophin central domain repeats 4 to 9

Dystrophin central domain repeats 4 to 9 experimental SAS data
NONE model
Sample: Dystrophin central domain repeats 4 to 9 monomer, 76 kDa Homo sapiens protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2012 Sep 19
Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions. J Biol Chem 293(18):6637-6646 (2018)
...Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, ...
RgGuinier 7.7 nm
Dmax 30.5 nm
VolumePorod 123 nm3

SASDB83 – Human dystrophin central domain repeats 16 to 17

Dystrophin central domain repeats 16 to 17. experimental SAS data
NONE model
Sample: Dystrophin central domain repeats 16 to 17. monomer, 28 kDa Homo sapiens protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2012 Sep 19
Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions. J Biol Chem 293(18):6637-6646 (2018)
...Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, ...
RgGuinier 3.1 nm
Dmax 13.0 nm
VolumePorod 47 nm3

SASDB93 – Human dystrophin central domain repeats 16 to 19

Dystrophin central domain repeats 16 to 19. experimental SAS data
NONE model
Sample: Dystrophin central domain repeats 16 to 19. monomer, 50 kDa Homo sapiens protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol 5% acetonitrile, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2013 Oct 4
Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions. J Biol Chem 293(18):6637-6646 (2018)
...Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, ...
RgGuinier 4.6 nm
Dmax 20.0 nm
VolumePorod 70 nm3

SASDBA3 – Human dystrophin central domain repeats 20 to 24

Dystrophin central domain repeats 20 to 24. experimental SAS data
NONE model
Sample: Dystrophin central domain repeats 20 to 24. monomer, 67 kDa Homo sapiens protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2011 Jul 10
Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions. J Biol Chem 293(18):6637-6646 (2018)
...Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, ...
RgGuinier 5.8 nm
Dmax 22.5 nm
VolumePorod 107 nm3

SASDBB3 – Human dystrophin central domain single repeat 23

Dystrophin central domain single repeat 23 experimental SAS data
NONE model
Sample: Dystrophin central domain single repeat 23 monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2011 Oct 7
Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions. J Biol Chem 293(18):6637-6646 (2018)
...Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, ...
RgGuinier 2.2 nm
Dmax 7.4 nm
VolumePorod 20 nm3

SASDBV3 – Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant)

Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant, deletion of exons 45-47) experimental SAS data
GASBOR model
Sample: Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant, deletion of exons 45-47) monomer, 64 kDa Homo sapiens protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol 5% acetonitrile, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2014 Feb 5
Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions. J Biol Chem 293(18):6637-6646 (2018)
...Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, ...
RgGuinier 6.0 nm
Dmax 21.0 nm
VolumePorod 184 nm3

SASDDJ9 – Conformation of the R1-3 human dystrophin fragment (SANS)

R1-3 human dystrophin fragment experimental SAS data
YASARA model
Sample: R1-3 human dystrophin fragment monomer, 39 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5, pH: 7.1
Experiment: SANS data collected at D22, ILL on 2016 Nov 7
Human Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids. Biophys J 115(7):1231-1239 (2018)
Dos Santos Morais R, Delalande O, Pérez J, Mias-Lucquin D, Lagarrigue M, Martel A, Molza AE, Chéron A, Raguénès-Nicol C, Chenuel T, Bondon A, Appavou MS, Le Rumeur E, Combet S, Hubert JF
RgGuinier 4.2 nm
Dmax 17.7 nm
VolumePorod 46 nm3

SASDDK9 – Conformation of R1-3 human dystrophin fragment in interaction with zwitterionic phospholipid bicelles (SANS)

R1-3 human dystrophin fragment experimental SAS data
DAMMIF model
Sample: R1-3 human dystrophin fragment monomer, 39 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5, pH: 7.1
Experiment: SANS data collected at D22, ILL on 2016 Nov 7
Human Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids. Biophys J 115(7):1231-1239 (2018)
Dos Santos Morais R, Delalande O, Pérez J, Mias-Lucquin D, Lagarrigue M, Martel A, Molza AE, Chéron A, Raguénès-Nicol C, Chenuel T, Bondon A, Appavou MS, Le Rumeur E, Combet S, Hubert JF
RgGuinier 4.1 nm
Dmax 17.8 nm
VolumePorod 50 nm3

SASDDL9 – Conformation of R1-3 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)

R1-3 human dystrophin fragment experimental SAS data
YASARA model
Sample: R1-3 human dystrophin fragment monomer, 39 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5, pH: 7.1
Experiment: SANS data collected at D22, ILL on 2016 Nov 7
Human Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids. Biophys J 115(7):1231-1239 (2018)
Dos Santos Morais R, Delalande O, Pérez J, Mias-Lucquin D, Lagarrigue M, Martel A, Molza AE, Chéron A, Raguénès-Nicol C, Chenuel T, Bondon A, Appavou MS, Le Rumeur E, Combet S, Hubert JF
RgGuinier 6.2 nm
Dmax 24.8 nm
VolumePorod 100 nm3

SASDFW4 – Conformation of R8-15 human dystrophin fragment

Human dystrophin central domain R8-15 fragment experimental SAS data
CUSTOM IN-HOUSE model
Sample: Human dystrophin central domain R8-15 fragment monomer, 100 kDa protein
Buffer: NaP 10 mM, NaCl 500 mM, EDTA 1 mM, Glycerol 2%, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2015 Sep 23
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids. J Struct Biol :107411 (2019)
...Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O
RgGuinier 10.1 nm
Dmax 36.0 nm

SASDFX4 – Conformation of R11-19 human dystrophin fragment

Human dystrophin central domain R11-19 fragment experimental SAS data
CUSTOM IN-HOUSE model
Sample: Human dystrophin central domain R11-19 fragment monomer, 117 kDa protein
Buffer: NaP 20 mM, NaCl 300 mM, EDTA 1 mM, Glycerol 2%, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2017 May 11
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids. J Struct Biol :107411 (2019)
...Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O
RgGuinier 8.8 nm
Dmax 37.5 nm
VolumePorod 513 nm3

SASDFT4 – Conformation of the R11-15 human dystrophin fragment (SANS)

Dystrophin (R11-15 human dystrophin fragment) experimental SAS data
CUSTOM IN-HOUSE model
Sample: Dystrophin (R11-15 human dystrophin fragment) monomer, 60 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH: 7.1
Experiment: SANS data collected at D22, ILL on 2016 Nov 1
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids. J Struct Biol :107411 (2019)
...Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O
RgGuinier 6.2 nm
Dmax 27.4 nm
VolumePorod 146 nm3

SASDFU4 – Conformation of R11-15 human dystrophin fragment in interaction with zwitterionic phospholipid bicelles (SANS)

Dystrophin (R11-15 human dystrophin fragment) experimental SAS data
DAMMIF model
Sample: Dystrophin (R11-15 human dystrophin fragment) monomer, 60 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH: 7.1
Experiment: SANS data collected at D22, ILL on 2016 Nov 1
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids. J Struct Biol :107411 (2019)
...Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O
RgGuinier 6.2 nm
Dmax 28.1 nm
VolumePorod 144 nm3

SASDFV4 – Conformation of R11-15 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)

Dystrophin (R11-15 human dystrophin fragment) experimental SAS data
DAMMIF model
Sample: Dystrophin (R11-15 human dystrophin fragment) monomer, 60 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH: 7.1
Experiment: SANS data collected at D22, ILL on 2016 Nov 1
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids. J Struct Biol :107411 (2019)
...Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O
RgGuinier 8.1 nm
Dmax 29.6 nm
VolumePorod 231 nm3