2. Measurements Reported by SASBDB Reported Results
Metric
Method
Value
Uncertainty
Unit
dmax
P(r)
7.06
—
Å
i0
Guinier
0.103287
0.000861426
—
i0
P(r)
0.106
0.001
—
mw
Experimental
4.587
—
kDa
mw
Porod
2.3
—
kDa
porod_volume
Porod
3.69
—
ų
rg
Guinier
1.657
0.168
Å
rg
P(r)
1.819
0.03
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/62/sasdc62/source/SASDC62.dat
downloaded
13961
full_entry_zip
sasbdb/entries/62/sasdc62/source/SASDC62.zip
downloaded
14853
pddf
sasbdb/entries/62/sasdc62/source/SASDC62.out
downloaded
35793
sascif
sasbdb/entries/62/sasdc62/source/SASDC62.sascif
downloaded
51466
summary
sasbdb/entries/62/sasdc62/source/summary.json
downloaded
6565
▶
5. Experiment Description and Publication Experiment & Publication
Original Experiment Description
SAXS data from solutions of the basic domain of telomeric repeat-binding factor 2 (TRF2) in 50 mM sodium phosphate, 50 mM NaCl, pH 7, were collected using a Rigaku BioSAXS-1000 instrument at CEITEC (Brno, Czech Republic) equipped with a Pilatus 100K detector at a sample-detector distance of 0.5 m (I(s) vs s, where = 4π sin θ/λ; 2θ is the scattering angle and λ = 0.154 nm). Six successive 3600 second frames were collected at a sample temperature of 4°C using a solute concentration of 1.2 mg/ml. The data were normalized to the intensity of the transmitted beam and radially averaged and the corresponding scattering from the solvent-blank was subtracted to produced the scattering profile displayed in this entry.
Related Publication
Title
Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it.
Authors
Necasová I, Janoušková E, Klumpler T, Hofr C
DOI / PMID
10.1093/nar/gkx812 / 28981702
▼
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.
CEITEC - Central European Institute of Technology, Masaryk University
experiment.contributor[0].affiliation[0].webpage
https://www.ceitec.eu/
experiment.contributor[0].contributor_name
Tomas
experiment.contributor[0].contributor_surname
Klumpler
experiment.contributor[0].orcid
null
experiment.concentration_method
null
experiment.concentration_unit
null
experiment.date
2015-03-05
experiment.storage_temperature
4.0
experiment.cell_temperature
4.0
experiment.exposure_time
3600.0
experiment.number_of_frames
6
experiment.wavelength
1.54
experiment.sample_detector_distance
0.48
experiment.concentration_min
null
experiment.concentration_max
1.2
experiment.sample_volume
null
experiment.flow_rate
null
experiment.s_min
0.109
experiment.s_max
6.503
experiment.total_exposure_time
null
experiment.seccolumn
null
fits
[]
estimated_volume_method
null
pddf_software
ATSAS GNOM
pddf_software_version
primus/qt r8972
i0_calibration_standard
null
description
null
experiment_description
SAXS data from solutions of the basic domain of telomeric repeat-binding factor 2 (TRF2) in 50 mM sodium phosphate, 50 mM NaCl, pH 7, were collected using a Rigaku BioSAXS-1000 instrument at CEITEC (Brno, Czech Republic) equipped with a Pilatus 100K detector at a sample-detector distance of 0.5 m (I(s) vs s, where = 4π sin θ/λ; 2θ is the scattering angle and λ = 0.154 nm). Six successive 3600 second frames were collected at a sample temperature of 4°C using a solute concentration of 1.2 mg/ml. The data were normalized to the intensity of the transmitted beam and radially averaged and the corresponding scattering from the solvent-blank was subtracted to produced the scattering profile displayed in this entry.