5. Experiment Description and Publication Experiment & Publication
Original Experiment Description
X-ray synchrotron radiation scattering data from solutions of Suppressor of Copper Sensitivity C protein (ScsC) protein from Proteus mirabilis in 10 mM HEPES 150mM NaCl, pH 7.4 were collected on the SAXS/WAXS beam line of the Australian Synchrotron (Melbourne, Australia) using a 2D Photon counting Pilatus 1M-W pixel detector (s = 4π sin θ/λ, where 2θ is the scattering angle). Thirty eight successive 1 second frames were collected across solute concentrations of 0.1-10.0 mg/ml at a sample temperature of 10°C. The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted. The SAXS data displayed this entry was derived from a 10.0 mg/ml sample and show that essentially only trimer is present in solution. A linear combination of monomer and trimer are fit to the scattering curve, and the final concentration of each species in solution was determined to be: 0.08 µM (monomer); 95.05 µM (trimer). Together, with data collected at other concentration (available to download as a zip archive), it was estimated that K1 (3monomer <-> trimer) was 6.3 nM^2.
Related Publication
Title
Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis.
Authors
Furlong EJ, Kurth F, Premkumar L, Whitten AE, Martin JL
DOI / PMID
10.1107/S2059798319000081 / 30950400
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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：159 field values
Field path
Raw value
code
SASDER4
status
Published
type_of_curve
Single concentration
angular_unit
1/A
project.title
Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis.
project.publication.title
Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis.
project.publication.author_list
Furlong EJ, Kurth F, Premkumar L, Whitten AE, Martin JL
Monomer concentration = 0.08 uM
Trimer concentration = 95.05 uM
estimated_volume_method
null
pddf_software
ATSAS GNOM
pddf_software_version
4.6
i0_calibration_standard
null
description
null
experiment_description
X-ray synchrotron radiation scattering data from solutions of Suppressor of Copper Sensitivity C protein (ScsC) protein from Proteus mirabilis in 10 mM HEPES 150mM NaCl, pH 7.4 were collected on the SAXS/WAXS beam line of the Australian Synchrotron (Melbourne, Australia) using a 2D Photon counting Pilatus 1M-W pixel detector (s = 4π sin θ/λ, where 2θ is the scattering angle). Thirty eight successive 1 second frames were collected across solute concentrations of 0.1-10.0 mg/ml at a sample temperature of 10°C. The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted. The SAXS data displayed this entry was derived from a 10.0 mg/ml sample and show that essentially only trimer is present in solution. A linear combination of monomer and trimer are fit to the scattering curve, and the final concentration of each species in solution was determined to be: 0.08 µM (monomer); 95.05 µM (trimer). Together, with data collected at other concentration (available to download as a zip archive), it was estimated that K1 (3monomer <-> trimer) was 6.3 nM^2.
