5. Experiment Description and Publication Experiment & Publication
Original Experiment Description
X-ray synchrotron radiation scattering data from solutions of the n-terminal domain of DsbD from Neisseria meningitidis in 25 mM HEPES 150mM NaCl pH 6.7 were collected on the SAXS/WAXS beam line of the Australian Synchrotron (Melbourne, Australia) using a 2D Photon counting Pilatus 1M-W pixel detector (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle; λ=0.1127 nm). Thirty successive 2 second frames were collected across solute concentrations of 0.4-5.9 mg/ml. The SAXS data displayed this entry was derived from a 0.74 mg/ml sample as it was deemed to be the highest concentration at which the effects of concentration were negligible. The Rg for n-NmDsbD showed mild concentration dependence above a concentration of 1.0 mg/mL, dropping from ~17.5 Å at 0.4 mg/mL to ~16 Å at 5.9 mg/mL. The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted. The models and corresponding fits include those derived from dummy-atom modelling using DAMMIN.
Related Publication
Title
Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis.
Authors
Smith RP, Whitten AE, Paxman JJ, Kahler CM, Scanlon MJ, Heras B
DOI / PMID
10.1107/S2053230X17017800 / 29372905
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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：156 field values
Field path
Raw value
code
SASDCH7
status
Published
type_of_curve
Single concentration
angular_unit
1/A
project.title
Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis.
project.publication.title
Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis.
project.publication.author_list
Smith RP, Whitten AE, Paxman JJ, Kahler CM, Scanlon MJ, Heras B
X-ray synchrotron radiation scattering data from solutions of the n-terminal domain of DsbD from Neisseria meningitidis in 25 mM HEPES 150mM NaCl pH 6.7 were collected on the SAXS/WAXS beam line of the Australian Synchrotron (Melbourne, Australia) using a 2D Photon counting Pilatus 1M-W pixel detector (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle; λ=0.1127 nm). Thirty successive 2 second frames were collected across solute concentrations of 0.4-5.9 mg/ml. The SAXS data displayed this entry was derived from a 0.74 mg/ml sample as it was deemed to be the highest concentration at which the effects of concentration were negligible. The Rg for n-NmDsbD showed mild concentration dependence above a concentration of 1.0 mg/mL, dropping from ~17.5 Å at 0.4 mg/mL to ~16 Å at 5.9 mg/mL. The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted. The models and corresponding fits include those derived from dummy-atom modelling using DAMMIN.
