Data type: SASBDB experimental dataStatus: PublishedCurve type: Single concentrationLast updated: 2025-06-16T15:29:56.969374+02:00
NOTE: The calculated Porod volume and estimated molecular weight determined from the SAXS profile (27-60 kDa) is significantly larger than that expected for a dimer (17 kDa).
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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)
19.0
0.5
Å
i0
Guinier
356.72
—
arbitrary
i0
P(r)
347.7
—
arbitrary
mw
Experimental
8.5
—
kDa
mw
Guinier I(0)
19.1
0.1
kDa
porod_volume
Porod
116.7
—
ų
rg
Guinier
4.495
1.516
Å
rg
P(r)
4.54
0.02
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/s6/sasdvs6/source/SASDVS6.dat
downloaded
34741
full_entry_zip
sasbdb/entries/s6/sasdvs6/source/SASDVS6.zip
downloaded
27494
pddf
sasbdb/entries/s6/sasdvs6/source/SASDVS6.out
downloaded
68852
sascif
sasbdb/entries/s6/sasdvs6/source/SASDVS6.sascif
not_available
—
summary
sasbdb/entries/s6/sasdvs6/source/summary.json
downloaded
6898
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5. Experiment Description and Publication Experiment & Publication
Original Experiment Description
Synchrotron SAXS data from solutions of the SARS-CoV-2 N-protein inter-domain linker (IDL, amino acids 176-245) in 100 mM Tris-HCl, 150 mM NaCl, 1 mM EDTA, pH 8 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.0999 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 14.00 mg/ml was measured at 10°C. 10 successive 2 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
Dynamic ensembles of SARS-CoV-2 N-protein reveal head-to-head coiled-coil-driven oligomerization and phase separation.
Strep(II)-tagged N-protein 176-245. The protein construct used for SAXS contains an additional two amino acids at the N-terminus (GP) as well as the VWSHPQFEK C-terminal tag.
Instituto de Tecnologia Química e Biológica António Xavier, Universidade de Lisboa
experiment.contributor[0].affiliation[0].webpage
http://www.itqb.unl.pt
experiment.contributor[0].contributor_name
Guillem
experiment.contributor[0].contributor_surname
Hernandez
experiment.contributor[0].orcid
https://orcid.org/0000-0003-4438-5611
experiment.concentration_method
null
experiment.concentration_unit
null
experiment.date
2023-01-29
experiment.storage_temperature
10.0
experiment.cell_temperature
10.0
experiment.exposure_time
2.0
experiment.number_of_frames
10
experiment.wavelength
0.0999
experiment.sample_detector_distance
2.8
experiment.concentration_min
null
experiment.concentration_max
14.0
experiment.sample_volume
null
experiment.flow_rate
null
experiment.s_min
0.203
experiment.s_max
4.183
experiment.total_exposure_time
null
experiment.seccolumn
null
fits
[]
estimated_volume_method
null
pddf_software
ATSAS GNOM
pddf_software_version
5.0
i0_calibration_standard
null
description
NOTE: The calculated Porod volume and estimated molecular weight determined from the SAXS profile (27-60 kDa) is significantly larger than that expected for a dimer (17 kDa).
experiment_description
Synchrotron SAXS data from solutions of the SARS-CoV-2 N-protein inter-domain linker (IDL, amino acids 176-245) in 100 mM Tris-HCl, 150 mM NaCl, 1 mM EDTA, pH 8 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.0999 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 14.00 mg/ml was measured at 10°C. 10 successive 2 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.