SASDCJ7

C-terminal domain of DsbD from N. meningitidis

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2021-04-10T09:51:59.686965+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · C-terminal domain of DsbD from N. meningitidis

Concentration0.3 – 4.5 Buffer / pH25mM HEPES 150mM NaCl / 6.7
Experimental temperature12.0 Facility / beamlineAustralian Synchrotron / SAXS/WAXS
Wavelength0.1127 nmExposure2.0 s × 30

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein)
View sequence
SNAARDNVTKSKISQYKDQIFDLTYPYSGNENSSVIAVGFLDYSCGHCKAIKNDIKQLINDGKIKYIFRDAPILGNASLKAAKSALAVYFLNKEKYFDFHHAALSHKGEFSDESILDIVKNIGIDEDDFNDSIKDNADKIEQMINNSRLLVRDLGVGGTPFLIIGDSLFVGATDLNVLRKKVDELSHKQG
proteinWolbachia endosymbiont of Drosophila melanogasterQ73FL665–252monomerMolecule count 121.091 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1299[3]0.0136047–0.398953 1/AHas uncertainty columnMissing 00sasbdb/entries/j7/sasdcj7/source/SASDCJ7.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)4.50.3Å
i0Guinier0.009972e-051/cm
i0P(r)0.0099051.1e-051/cm
mwExperimental11.8—kDa
mwGuinier I(0)11.81.0kDa
mwPorod12.0—kDa
porod_volumePorod14.6—ų
rgGuinier1.530.01Å
rgP(r)14.80.1Å

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

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4. Source File Index Source Files

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5. Experiment Description and Publication Experiment & Publication

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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.

Open the original SASBDB entry

Buffer and Sample Properties

Buffer name25mM HEPES 150mM NaClBuffer concentration—
pH6.7Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2013-05-04Storage / measurement temperature4.0 / 12.0
Exposure time2.0Frames30
Wavelength0.1127Sample-to-detector distance1.48
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineAustralian Synchrotron / SAXS/WAXS · Melbourne, Australia
q range0.136 – 3.99Sample volume / flow rate— / —

Original SASBDB Plots

Experimental I(q)
Experimental I(q)
Experimental I(q), log-log
Experimental I(q), log-log
Guinier plot
Guinier plot
Kratky plot
Kratky plot
P(r) plot
P(r) plot

Downloadable Files

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All source fields (unfiltered)

Every source field is expanded here, including empty values, list members and fields already shown above.

summary.json:156 field values
Field pathRaw value
codeSASDCJ7
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleProduction, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis.
project.publication.titleProduction, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis.
project.publication.author_listSmith RP, Whitten AE, Paxman JJ, Kahler CM, Scanlon MJ, Heras B
project.publication.journalActa Crystallogr F Struct Biol Commun
project.publication.doi10.1107/S2053230X17017800
project.publication.pmid29372905
project.publication.published_date2018 Jan 1
project.statusreleased
project.submitted_date2017-09-13
project.released_date2018-01-03
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experiment.instrument.detector.namePilatus 1M
experiment.instrument.detector.resolution172.0
experiment.instrument.nameAustralian Synchrotron
experiment.instrument.cityMelbourne
experiment.instrument.countryAustralia
experiment.instrument.beamline_nameSAXS/WAXS
experiment.instrument.beam_geometryPoint
experiment.instrument.type_of_sourceX-ray synchrotron
experiment.instrument.point_sourceTrue
experiment.instrument.line_collimationnull
experiment.instrument.sample_path_lengthnull
experiment.instrument.line_collimation_slitlengthnull
experiment.instrument.line_collimation_integrationwidthnull
experiment.instrument.xray_energynull
experiment.instrument.beam_profile_ahnull
experiment.instrument.beam_profile_alnull
experiment.sample.molecule[0].long_nameDsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein)
experiment.sample.molecule[0].short_nameα-DsbA2
experiment.sample.molecule[0].sequenceSNAARDNVTKSKISQYKDQIFDLTYPYSGNENSSVIAVGFLDYSCGHCKAIKNDIKQLINDGKIKYIFRDAPILGNASLKAAKSALAVYFLNKEKYFDFHHAALSHKGEFSDESILDIVKNIGIDEDDFNDSIKDNADKIEQMINNSR LLVRDLGVGGTPFLIIGDSLFVGATDLNVLRKKVDELSHKQG
experiment.sample.molecule[0].organismWolbachia endosymbiont of Drosophila melanogaster
experiment.sample.molecule[0].uniprot_codeQ73FL6
experiment.sample.molecule[0].uniprot_range_first65
experiment.sample.molecule[0].uniprot_range_last252
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMSRISFLLILIIAIASLPIINNWLSNRSQMLNDDYIGEKLDNYISRNFDKIVKTLKEESI KSSYAARDNVTKSKISQYKDQIFDLTYPYSGNENSSVIAVGFLDYSCGHCKAIKNDIKQL INDGKIKYIFRDAPILGNASLKAAKSALAVYFLDKEKYFDFHHAALSHKGEFSDESILDI VKNIGIDEDDFNDSIKDNADKIEQMINNSRLLVRDLGVGGTPFLIIGDSLFVGATDLNVL RKKVDELSHKQG
experiment.sample.molecule[0].mw21.091
experiment.sample.molecule[0].total_mw21.093
experiment.sample.molecule[0].number_molecules1
experiment.sample.molecule[0].complex_stateFalse
experiment.sample.molecule[0].deuterationnull
experiment.sample.molecule[0].molecule_sourcebiological
experiment.sample.molecule[0].molecule_descriptionnull
experiment.sample.buffer.name25mM HEPES 150mM NaCl
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph6.7
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameC-terminal domain of DsbD from N. meningitidis
experiment.sample.ext_coefficientnull
experiment.sample.contrastnull
experiment.sample.specific_volnull
experiment.sample.dry_volnull
experiment.sample.absorbptionnull
experiment.sample.deuterationnull
experiment.sample.mixturenull
experiment.contributor[0].affiliation[0].short_nameANSTO
experiment.contributor[0].affiliation[0].addressKirrawee DC, NSW 2232, Australia
experiment.contributor[0].affiliation[0].full_nameAustralian Nuclear Science and Technology Organisation
experiment.contributor[0].affiliation[0].webpage
experiment.contributor[0].contributor_nameAndrew
experiment.contributor[0].contributor_surnameWhitten
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2013-05-04
experiment.storage_temperature4.0
experiment.cell_temperature12.0
experiment.exposure_time2.0
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experiment.wavelength0.1127
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experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].softwareDAMMIN
fits[0].models[0].pdb_link[]
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pddf_softwareATSAS GNOM
pddf_software_version4.6
i0_calibration_standardnull
descriptionnull
experiment_descriptionX-ray synchrotron radiation scattering data from solutions of the c-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 0.3-4.5 mg/ml. The SAXS data displayed this entry was derived from a 1.12 mg/ml sample. The change in Rg for c-NmDsbD showed no obvious systematic trend in the concentration range measured. 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.
tags[]
intensity_unit1/cm
experimental_mw11.8
experimental_mw_errornull
guinier_i0_mw11.8
guinier_i0_mw_error1.0
porod_mw12.0
porod_mw_errornull
pddf_i00.009905
pddf_i0_error1.1e-05
guinier_i00.00997
guinier_i0_error2e-05
pddf_rg14.8
pddf_rg_error0.1
guinier_rg1.53
guinier_rg_error0.01
pddf_dmax4.5
pddf_dmax_error0.3
porod_volume14.6
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first2
guinier_point_last44
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDCJ7_datloglog_img.png
symmetrynull
last_modified2021-04-10T09:51:59.686965+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDCJ7
statussuccess
started_at2026-08-11T15:30:52.782754+00:00
finished_at2026-08-11T15:31:03.178383+00:00
source_last_modified2021-04-10T09:51:59.686965+02:00
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View the complete summary.json source
{
  "code": "SASDCJ7",
  "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.",
    "publication": {
      "title": "Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis.",
      "author_list": "Smith RP, Whitten AE, Paxman JJ, Kahler CM, Scanlon MJ, Heras B",
      "journal": "Acta Crystallogr F Struct Biol Commun",
      "doi": "10.1107/S2053230X17017800",
      "pmid": "29372905",
      "published_date": "2018 Jan 1"
    },
    "status": "released",
    "submitted_date": "2017-09-13",
    "released_date": "2018-01-03"
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      },
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      "name": "C-terminal domain of DsbD from N. meningitidis",
      "ext_coefficient": null,
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View the complete manifest.json source
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