2. Measurements Reported by SASBDB Reported Results
Metric
Method
Value
Uncertainty
Unit
dmax
P(r)
18.0
—
Å
i0
Guinier
46.42
1.0
1/cm
i0
P(r)
49.16
—
1/cm
mw
Experimental
24.49
—
kDa
porod_volume
Porod
133.0
—
ų
rg
Guinier
3.74
0.1
Å
rg
P(r)
4.39
—
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/u7/sasdeu7/source/SASDEU7.dat
downloaded
25923
full_entry_zip
sasbdb/entries/u7/sasdeu7/source/SASDEU7.zip
downloaded
16497
pddf
sasbdb/entries/u7/sasdeu7/source/SASDEU7.out
downloaded
29890
sascif
sasbdb/entries/u7/sasdeu7/source/SASDEU7.sascif
downloaded
62963
summary
sasbdb/entries/u7/sasdeu7/source/summary.json
downloaded
6478
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5. Experiment Description and Publication Experiment & Publication
Original Experiment Description
Synchrotron SAXS data from solutions of the stator protein FlaG soluble domain in 25 mM citric acid/sodium citrate, 150mM NaCl, 3% glycerol, pH 3 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 1.5 m and at a wavelength of λ = 0.127 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.5 and 5 mg/ml were measured at 10°C. 33 successive 0.300 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
The structure of the periplasmic FlaG-FlaF complex and its essential role for archaellar swimming motility.
Authors
Tsai CL, Tripp P, Sivabalasarma S, Zhang C, Rodriguez-Franco M, Wipfler RL, Chaudhury P, Banerjee A, Beeby M, Whitaker RJ, Tainer JA, Albers SV
DOI / PMID
10.1038/s41564-019-0622-3 / 31844299
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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 the stator protein FlaG soluble domain in 25 mM citric acid/sodium citrate, 150mM NaCl, 3% glycerol, pH 3 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 1.5 m and at a wavelength of λ = 0.127 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.5 and 5 mg/ml were measured at 10°C. 33 successive 0.300 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.