2. Measurements Reported by SASBDB Reported Results
Metric
Method
Value
Uncertainty
Unit
dmax
P(r)
10.0
—
nm
i0
Guinier
0.142456
—
1/cm
mw
Experimental
62.4
—
kDa
mw
Porod
70.0
—
kDa
porod_volume
Porod
112.0
—
nm³
rg
Guinier
2.87
0.007
nm
These values are reported by SASBDB; SAXSdb did not recalculate them from the experimental curve.
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3. Source Fits and Models Source Fits & Models
This entry has no source fit record.
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4. Source File Index Source Files
Category
Path
Download status
Size
curve
sasbdb/entries/l3/sasdxl3/source/SASDXL3.dat
downloaded
137944
full_entry_zip
sasbdb/entries/l3/sasdxl3/source/SASDXL3.zip
downloaded
40635
pddf
sasbdb/entries/l3/sasdxl3/source/SASDXL3.out
not_listed
—
sascif
sasbdb/entries/l3/sasdxl3/source/SASDXL3.sascif
not_available
—
summary
sasbdb/entries/l3/sasdxl3/source/summary.json
downloaded
7051
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5. Experiment Description and Publication Experiment & Publication
Original Experiment Description
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.
Related Publication
Title
Unveiling the structure, function and dynamics of StmPr1 in Stenotrophomonas maltophilia virulence.
Authors
Sommer M, Negm A, Outzen L, Windhorst S, Gabdulkhakov A, Weber W, Betzel C
DOI / PMID
10.1038/s41598-025-06177-5 / 40542111
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6. Complete Source Record Complete Source Record
The following content comes directly from the SASBDB entry. Missing values are shown as “—”; SAXSdb does not infer undeclared units.
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.