Improving data quality and expanding BioSAXS experiments to low-molecular-weight and low-concentration protein samples.

Castellví A, Pascual-Izarra C, Crosas E, Malfois M, Juanhuix J, Acta Crystallogr D Struct Biol 76(Pt 10):971-981 (2020) Europe PMC

SASDJH3 – Hen Egg White Lysozyme in presence of 100 mM 5-methyl uridine

Lysozyme C
MWexperimental 16 kDa
MWexpected 16 kDa
VPorod 21 nm3
log I(s) 2.10×100 2.10×10-1 2.10×10-2 2.10×10-3
Lysozyme C small angle scattering data  s, nm-1
ln I(s)
Lysozyme C Guinier plot ln 2.10×100 Rg: 1.5 nm 0 (1.5 nm)-2 s2
(sRg)2I(s)/I(0)
Lysozyme C Kratky plot 1.104 0 √3 sRg
Dmax: 4.2 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from a solution of 7.00 mg/ml human Hen Egg White Lysozyme (HEWL) in 40 mM sodium acetate pH 3.8, 150 mM NaCl, 100 mM 5-methyl uridine was collected on the BL11-NCD-SWEET beam line at ALBA Synchrotron using a Pilatus 1M photon-counting detector. The beam at sample position was 0.35 mm (horizontal) × 0.38 mm (vertical), the incident photon flux was 7.6×10e11 photons/s at 12.4 keV (λ =0.0999 nm) and the sample to detector distance was 2.291 m. 2000 successive 0.1 second frames were collected and data were normalized to the intensity of the transmitted beam and radially averaged. The current buffer-subtracted scattering profile corresponds to the average of 225 collected frames. The absorbed dose by the sample was 13.50 kGy.

Sample temperature: 25°C. CAUTION! The scattering intensities do not have associated errors.

Lysozyme C (LYZ)
Mol. type   Protein
Organism   Gallus gallus
Olig. state   Monomer
Mon. MW   16.2 kDa
 
UniProt   P00698 (1-147)
Sequence   FASTA