Browse by MODEL: Hybrid

SASDMD2 – SWAXS data from Lysozyme Solution [Protein concentration 2.5 mg/ml] at 10 °C

Lysozyme C experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM NaOAc pH 3.8, 150 mM NaCl, pH: 3.8
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 May 2
Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme. J Biomol Struct Dyn :1-15 (2021)
Ashish
RgGuinier 1.4 nm
Dmax 4.3 nm

SASDME2 – SWAXS data from Lysozyme Solution [Protein concentration 1.8 mg/ml] at 10 °C

Lysozyme C experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM NaOAc pH 3.8, 150 mM NaCl, pH: 3.8
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 May 2
Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme. J Biomol Struct Dyn :1-15 (2021)
Ashish
RgGuinier 1.4 nm
Dmax 4.5 nm

SASDMF2 – SWAXS data from Lysozyme Solution [Protein concentration 0.9 mg/ml] at 10 °C

Lysozyme C experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM NaOAc pH 3.8, 150 mM NaCl, pH: 3.8
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 May 2
Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme. J Biomol Struct Dyn :1-15 (2021)
Ashish
RgGuinier 1.4 nm
Dmax 5.0 nm

SASDMG2 – SWAXS data from Lysozyme Solution [Protein concentration 0.4 mg/ml] at 10 °C

Lysozyme C experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM NaOAc pH 3.8, 150 mM NaCl, pH: 3.8
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 May 2
Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme. J Biomol Struct Dyn :1-15 (2021)
Ashish
RgGuinier 1.5 nm
Dmax 4.6 nm

SASDMH2 – SAXS Data of Lysozyme (Average of 0.9, 1.8, 2.5 and 5 mg/ml) Analyzed in the q range of 0.08-2.75 1/nm

Lysozyme C experimental SAS data
DAMMIF model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM NaOAc pH 3.8, 150 mM NaCl, pH: 3.8
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 May 2
Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme. J Biomol Struct Dyn :1-15 (2021)
Ashish
RgGuinier 1.4 nm
Dmax 4.2 nm

SASDMJ2 – SAXS Data of Lysozyme (Average of 0.9, 1.8, 2.5 and 5 mg/ml) Analyzed in the q range of 0.08-4.95 1/nm

Lysozyme C experimental SAS data
DAMMIF model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM NaOAc pH 3.8, 150 mM NaCl, pH: 3.8
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 May 2
Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme. J Biomol Struct Dyn :1-15 (2021)
Ashish
RgGuinier 1.4 nm
Dmax 4.2 nm

SASDMK2 – SWAXS Data of Lysozyme (Average of 0.9, 1.8, 2.5 and 5 mg/ml) Analyzed in the q range of 0.08-9.9 1/nm

Lysozyme C experimental SAS data
DAMMIF model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM NaOAc pH 3.8, 150 mM NaCl, pH: 3.8
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 May 2
Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme. J Biomol Struct Dyn :1-15 (2021)
Ashish
RgGuinier 1.4 nm
Dmax 4.2 nm

SASDML2 – SWAXS Data of Lysozyme (Average of 0.9, 1.8, 2.5 and 5 mg/ml) Analyzed in the q range of 0.08-17.2 1/nm

Lysozyme C experimental SAS data
DAMMIF model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM NaOAc pH 3.8, 150 mM NaCl, pH: 3.8
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 May 2
Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme. J Biomol Struct Dyn :1-15 (2021)
Ashish
RgGuinier 1.4 nm
Dmax 4.2 nm

SASDGW5 – Suppressor of Fused from Drosophila

Suppressor of fused homolog experimental SAS data
CUSTOM IN-HOUSE model
Sample: Suppressor of fused homolog monomer, 53 kDa Drosophila melanogaster protein
Buffer: 50 mM bis-TRIS pH 5.5, 200 mM NaCl, 10% glycerol, pH: 5.5
Experiment: SAXS data collected at SWING, SOLEIL on 2012 May 7
Suppressor of Fused
Valerie Biou
RgGuinier 2.7 nm
Dmax 8.8 nm
VolumePorod 12 nm3

SASDGZ5 – Suppressor of Fused from Human D30

Suppressor of fused homolog experimental SAS data
CUSTOM IN-HOUSE model
Sample: Suppressor of fused homolog monomer, 51 kDa Homo sapiens protein
Buffer: 50 mM bis-TRIS pH 5.5, 200 mM NaCl, 10% glycerol, pH: 5.5
Experiment: SAXS data collected at SWING, SOLEIL on 2018 Jun 30
Suppressor of Fused
Valerie Biou
RgGuinier 3.2 nm
Dmax 14.0 nm