SASDJP7 – Cysteine desulfurase, Iron-sulfur cluster assembly protein, Protein ISD11 (IscS_IscU_Isd11) complex

Cysteine desulfurase, putativeIron-sulfur cluster assembly proteinProtein ISD11 experimental SAS data
DAMMIF model
Sample: Cysteine desulfurase, putative tetramer, 204 kDa Plasmodium falciparum (isolate … protein
Iron-sulfur cluster assembly protein tetramer, 56 kDa Plasmodium falciparum (isolate … protein
Protein ISD11 tetramer, 43 kDa Plasmodium falciparum (isolate … protein
Buffer: 50 mM Tris-Cl, 300 mM NaCl, 5% Glycerol, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2019 Sep 19
[Fe-S] cluster biogenesis and unusual assembly of the ISC scaffold complex in Plasmodium falciparum mitochondrion
Ravishankar Ramachandran
RgGuinier 7.1 nm
Dmax 17.9 nm
VolumePorod 950 nm3

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

SASDMC2 – SWAXS data from Lysozyme Solution [Protein concentration 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 1.3 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

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

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

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

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

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

4122 hits found.