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8 hits found for Combet

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, Institut Laue-Langevin (ILL) on 2016 Nov 7
Human Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids. Biophys J 115(7):1231-1239 (2018)
...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, Institut Laue-Langevin (ILL) on 2016 Nov 7
Human Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids. Biophys J 115(7):1231-1239 (2018)
...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, Institut Laue-Langevin (ILL) on 2016 Nov 7
Human Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids. Biophys J 115(7):1231-1239 (2018)
...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)
...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)
...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, Institut Laue-Langevin (ILL) on 2016 Nov 1
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids. J Struct Biol :107411 (2019)
...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, Institut Laue-Langevin (ILL) on 2016 Nov 1
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids. J Struct Biol :107411 (2019)
...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, Institut Laue-Langevin (ILL) on 2016 Nov 1
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids. J Struct Biol :107411 (2019)
...Combet S, Hubert JF, Delalande O
RgGuinier 8.1 nm
Dmax 29.6 nm
VolumePorod 231 nm3