Visram Z,
Kestemont D,
Bauer B,
Qiao R,
Durica-Mitic S,
Majoros-Hashempour A,
Schmidt J,
Berdaguer R,
Krey K,
Mutti M,
Zerbs M,
von Freyberg M,
Corsini L,
Badarau AFrontiers in Microbiology
17
(2026)
DOI
SASDZ88 – Synthetic fusion protein comprising human IgG1 Fc, the CHAP domain of engineered Staphylococcus aureus LytN, and engineered Staphylococcus simulans lysostaphin (Fc-L2a-CHAP(alt)-LSN(HEK))
Synchrotron SAXS
data from solutions of
Synthetic fusion protein comprising human IgG1 Fc, the CHAP domain of engineered Staphylococcus aureus LytN, and engineered Staphylococcus simulans lysostaphin (Fc-L2a-CHAP(alt)-LSN(HEK))
in
20 mM HEPES, 150 mM NaCl, pH 7.0, pH 7
were collected
on the
EMBL P12 beam line
at the PETRA III storage ring
(DESY; Hamburg, Germany)
using a Pilatus 6M detector
at a sample-detector distance of 3 m and
at a wavelength of λ = 0.124 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 25.00 μl sample
at 5 mg/ml was injected at a 0.35 ml/min flow rate
onto a Cytiva Superdex 200 Increase 5/150 column
at 25°C.
1800 successive
0.500 second frames were collected.
The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
s, nm-1
