2. Measurements Reported by SASBDB Reported Results
Metric
Method
Value
Uncertainty
Unit
dmax
P(r)
13.0
—
Å
i0
Guinier
1.99
0.01
arbitrary
i0
P(r)
1.987
—
arbitrary
mw
Experimental
59.1
—
kDa
mw
Guinier I(0)
47.0
5.0
kDa
porod_volume
Porod
129.0
—
ų
rg
Guinier
3.51
0.11
Å
rg
P(r)
3.55
—
Å
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/55/sasdg55/source/SASDG55.dat
downloaded
20598
full_entry_zip
sasbdb/entries/55/sasdg55/source/SASDG55.zip
downloaded
18505
pddf
sasbdb/entries/55/sasdg55/source/SASDG55.out
downloaded
47604
sascif
sasbdb/entries/55/sasdg55/source/SASDG55.sascif
downloaded
62349
summary
sasbdb/entries/55/sasdg55/source/summary.json
downloaded
6743
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5. Experiment Description and Publication Experiment & Publication
Original Experiment Description
Synchrotron SAXS data from solutions of deglycosylated latency associated peptide (LAP) from the transforming growth factor beta-1 proprotein (TGFB-1) in phosphate buffered saline, 2% glycerol, pH 7.4 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.127 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.40 mg/ml was measured at 10°C. 100 successive 0.100 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.
Related Publication
Title
Structural insights into conformational switching in latency-associated peptide between transforming growth factor β-1 bound and unbound states
Authors
Stachowski T, Snell M, Snell E
DOI / PMID
10.1107/S205225251901707X / —
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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 deglycosylated latency associated peptide (LAP) from the transforming growth factor beta-1 proprotein (TGFB-1) in phosphate buffered saline, 2% glycerol, pH 7.4 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.127 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.40 mg/ml was measured at 10°C. 100 successive 0.100 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.