Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme.

Ashish
J Biomol Struct Dyn :1-15 (2021 Sep 25)

PMID: 34569414 doi: 10.1080/07391102.2021.1977704

Submitted to SASBDB: 2021 Aug 17 Published in SASBDB: 2021 Sep 28

SASDMC2 – SWAXS data from Lysozyme Solution [Protein concentration 5 mg/ml] at 10 °C 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 RgGuinier 1.3 nm Dmax 4.2 nm

SASDMD2 – SWAXS data from Lysozyme Solution [Protein concentration 2.5 mg/ml] at 10 °C 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 RgGuinier 1.4 nm Dmax 4.3 nm

SASDME2 – SWAXS data from Lysozyme Solution [Protein concentration 1.8 mg/ml] at 10 °C 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 RgGuinier 1.4 nm Dmax 4.5 nm

SASDMF2 – SWAXS data from Lysozyme Solution [Protein concentration 0.9 mg/ml] at 10 °C 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 RgGuinier 1.4 nm Dmax 5.0 nm

SASDMG2 – SWAXS data from Lysozyme Solution [Protein concentration 0.4 mg/ml] at 10 °C 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 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 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 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 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 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 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 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 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 RgGuinier 1.4 nm Dmax 4.2 nm