2. Measurements Reported by SASBDB Reported Results
Metric
Method
Value
Uncertainty
Unit
dmax
P(r)
12.0
—
Å
i0
Guinier
0.00477
4.1e-05
1/cm
i0
P(r)
0.004866
—
1/cm
mw
Experimental
15.8
—
kDa
mw
Porod
18.0
—
kDa
porod_volume
Porod
29.5
—
ų
rg
Guinier
2.429
0.2
Å
rg
P(r)
2.63
—
Å
These values are reported by SASBDB; SAXSdb did not recalculate them from the experimental curve.
▼
3. Source Fits and Models Source Fits & Models
This entry has no source fit record.
▶
4. Source File Index Source Files
Category
Path
Download status
Size
curve
sasbdb/entries/x4/sasdex4/source/SASDEX4.dat
downloaded
30902
full_entry_zip
sasbdb/entries/x4/sasdex4/source/SASDEX4.zip
downloaded
22580
pddf
sasbdb/entries/x4/sasdex4/source/SASDEX4.out
downloaded
46918
sascif
sasbdb/entries/x4/sasdex4/source/SASDEX4.sascif
downloaded
60220
summary
sasbdb/entries/x4/sasdex4/source/summary.json
downloaded
6404
▶
5. Experiment Description and Publication Experiment & Publication
Original Experiment Description
Synchrotron SAXS data from solutions of Herpes simplex virus 1 tegument protein UL11 in 50 mM HEPES, 100 mM NaCl, 0.5 mM tris(2-carboxyethyl)phosphine (TCEP), pH 7.5, were collected on the G1 beam line at the Cornell High Energy Synchrotron Source (CHESS, Ithaca, NY, USA) using a Pilatus 200K detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.124612 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Size exclusion chromatography SAXS (SEC-SAXS) was performed at 25°C using a sample injection concentration of 18.00 mg/ml. 497 successive 2 second data frames were collected through the SEC elution profile. Data corresponding to the UL11 elution peak were normalized to the intensity of the transmitted beam and radially averaged. Normalized and reduced SAXS data corresponding to solvent-blank ('solute-free' buffer) from the SEC column were subtracted.
Related Publication
Title
Conserved Outer Tegument Component UL11 from Herpes Simplex Virus 1 Is an Intrinsically Disordered, RNA-Binding Protein.
Authors
Metrick CM, Koenigsberg AL, Heldwein EE
DOI / PMID
10.1128/mBio.00810-20 / 32371601
▼
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 Herpes simplex virus 1 tegument protein UL11 in 50 mM HEPES, 100 mM NaCl, 0.5 mM tris(2-carboxyethyl)phosphine (TCEP), pH 7.5, were collected on the G1 beam line at the Cornell High Energy Synchrotron Source (CHESS, Ithaca, NY, USA) using a Pilatus 200K detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.124612 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Size exclusion chromatography SAXS (SEC-SAXS) was performed at 25°C using a sample injection concentration of 18.00 mg/ml. 497 successive 2 second data frames were collected through the SEC elution profile. Data corresponding to the UL11 elution peak were normalized to the intensity of the transmitted beam and radially averaged. Normalized and reduced SAXS data corresponding to solvent-blank ('solute-free' buffer) from the SEC column were subtracted.