2. Measurements Reported by SASBDB Reported Results
Metric
Method
Value
Uncertainty
Unit
i0
Guinier
10844.0
16.0
—
mw
Experimental
41.0
—
kDa
rg
Guinier
3.6
0.1
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/c6/sasddc6/source/SASDDC6.dat
downloaded
81699
full_entry_zip
sasbdb/entries/c6/sasddc6/source/SASDDC6.zip
downloaded
24050
pddf
sasbdb/entries/c6/sasddc6/source/SASDDC6.out
not_listed
—
sascif
sasbdb/entries/c6/sasddc6/source/SASDDC6.sascif
downloaded
103708
summary
sasbdb/entries/c6/sasddc6/source/summary.json
downloaded
6774
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5. Experiment Description and Publication Experiment & Publication
Original Experiment Description
Synchrotron SAXS data from solutions of the small glutamine-rich tetratricopeptide repeat-containing protein alpha (N-terminal-TPR domains; SGTA_NT) in 10 mM potassium phosphate, 100 mM NaCl, pH 6, were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY, Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.6 and 4.5 mg/ml were measured at 25°C. 20 successive 0.045 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
Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control.
Authors
Martínez-Lumbreras S, Krysztofinska EM, Thapaliya A, Spilotros A, Matak-Vinkovic D, Salvadori E, Roboti P, Nyathi Y, Muench JH, Roessler MM, Svergun DI, High S, Isaacson RL
DOI / PMID
10.1186/s12915-018-0542-3 / 29996828
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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.
Every source field is expanded here, including empty values, list members and fields already shown above.
summary.json:134 field values
Field path
Raw value
code
SASDDC6
status
Published
type_of_curve
Merged
angular_unit
1/nm
project.title
Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control.
project.publication.title
Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control.
project.publication.author_list
Martínez-Lumbreras S, Krysztofinska EM, Thapaliya A, Spilotros A, Matak-Vinkovic D, Salvadori E, Roboti P, Nyathi Y, Muench JH, Roessler MM, Svergun DI, High S, Isaacson RL
Synchrotron SAXS data from solutions of the small glutamine-rich tetratricopeptide repeat-containing protein alpha (N-terminal-TPR domains; SGTA_NT) in 10 mM potassium phosphate, 100 mM NaCl, pH 6, were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY, Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.6 and 4.5 mg/ml were measured at 25°C. 20 successive 0.045 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.