Data type: SASBDB experimental dataStatus: PublishedCurve type: SEC-SASLast updated: 2019-12-06T13:07:15.624532+01:00
The protein construct encompasses the dehydrogenase domain plus an additional upstream native-sequence amino acid linker (compare to the isolated dehydrogenase domain, SASDFV3, NPAC delta-261).
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1. Samples, Components and Experimental Conditions Sample & Experiment
2. Measurements Reported by SASBDB Reported Results
Metric
Method
Value
Uncertainty
Unit
dmax
P(r)
11.36
—
nm
i0
Guinier
24.1
0.09
arbitrary
i0
P(r)
24.0
—
arbitrary
mw
Experimental
160.0
—
kDa
mw
Porod
150.0
—
kDa
porod_volume
Porod
240.0
—
nm³
rg
Guinier
4.04
0.02
nm
rg
P(r)
4.015
—
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/w3/sasdfw3/source/SASDFW3.dat
downloaded
29641
full_entry_zip
sasbdb/entries/w3/sasdfw3/source/SASDFW3.zip
downloaded
20226
pddf
sasbdb/entries/w3/sasdfw3/source/SASDFW3.out
downloaded
40912
sascif
sasbdb/entries/w3/sasdfw3/source/SASDFW3.sascif
downloaded
64198
summary
sasbdb/entries/w3/sasdfw3/source/summary.json
downloaded
7406
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5. Experiment Description and Publication Experiment & Publication
Original Experiment Description
Synchrotron SAXS data from solutions of truncated cytokine-like nuclear factor (NPAC delta-205) in 15 mM HEPES, 200 mM NaCl, pH 7.3 were collected using size-exclusion chromatography SAXS (SEC-SAXS) on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). SEC-SAXS was performed at 20 °C using the following parameters: Column: Wyatt WTC-030N5; Flow rate: 0.25 mL/min; Sample injection concentration: 2 mg/mL; Injection volume: 50 μL. The data were collected through the SEC peak of the sample as a series of 222 x 1 second exposures. Each unsubtracted data frame was normalised to the intensity of the transmitted beam and radially averaged and the scattering of an appropriate solvent-blank was subtracted. The resulting subtracted frames were scaled and averaged to generate the final SAXS profile displayed in this entry.
Related Publication
Title
A Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC Multimeric Complex.
The protein construct encompasses the dehydrogenase domain plus an additional upstream native-sequence amino acid linker (compare to the isolated dehydrogenase domain, SASDFV3, NPAC delta-261).
experiment_description
Synchrotron SAXS data from solutions of truncated cytokine-like nuclear factor (NPAC delta-205) in 15 mM HEPES, 200 mM NaCl, pH 7.3 were collected using size-exclusion chromatography SAXS (SEC-SAXS) on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). SEC-SAXS was performed at 20 °C using the following parameters: Column: Wyatt WTC-030N5; Flow rate: 0.25 mL/min; Sample injection concentration: 2 mg/mL; Injection volume: 50 μL. The data were collected through the SEC peak of the sample as a series of 222 x 1 second exposures. Each unsubtracted data frame was normalised to the intensity of the transmitted beam and radially averaged and the scattering of an appropriate solvent-blank was subtracted. The resulting subtracted frames were scaled and averaged to generate the final SAXS profile displayed in this entry.