Unveiling the structure, function and dynamics of StmPr1 in Stenotrophomonas maltophilia virulence.

Sommer M, Negm A, Outzen L, Windhorst S, Gabdulkhakov A, Weber W, Betzel C, Sci Rep 15(1):20193 (2025) Europe PMC

SASDXL3 – Alkaline serine protease (47 kDa peptidase core and C-terminal domains, StmPr1)

Alkaline serine protease (Δ1-150)
MWexperimental 62 kDa
MWexpected 47 kDa
VPorod 112 nm3
log I(s) 1.42×10-1 1.42×10-2 1.42×10-3 1.42×10-4
Alkaline serine protease (Δ1-150) small angle scattering data  s, nm-1
ln I(s)
Alkaline serine protease (Δ1-150) Guinier plot ln 1.42×10-1 Rg: 2.9 nm 0 (2.9 nm)-2 s2
(sRg)2I(s)/I(0)
Alkaline serine protease (Δ1-150) Kratky plot 1.104 0 3 sRg
Dmax: 10 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of alkaline serine protease (peptidase core and C-terminal domains) in 20 mM Tris, 150 mM NaCl, pH 8 were collected on the EMBL P12 beam line at PETRA III (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.3 and 2 mg/ml were measured at 20°C. 20 successive 0.050 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Alkaline serine protease (Δ1-150) (StmPr1)
Mol. type   Protein
Organism   Stenotrophomonas maltophilia
Olig. state   Monomer
Mon. MW   47.5 kDa
 
UniProt   Q93IQ4 (151-617)
Sequence   FASTA