SASDEK4

C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein (ScsC)

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2020-06-15T11:37:11.282615+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein (ScsC)

Concentration— – 0.5 Buffer / pH10mM HEPES, 150mM NaCl / 7.4
Experimental temperature10.0 Facility / beamlineAustralian Synchrotron / SAXS/WAXS
Wavelength0.1033 nmExposure1.0 s × 38

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein
View sequence
SNAQFRQALASEHDALYNDAASPRIGAKDAKLVLVSFTDYNCPYCKRFDPLLEKITEQYPDVAVIIKPLPFKGESSAKASQAVLSVWKEDPKAFLALHQRLMQKKTMLDNASIEDAMKSTNTSKIKLTDDSLKTLQNNLELSRKLGIQGTPATVIGDTILPGAVDYDQLEIIVKEQLAKVKK
proteinProteus mirabilisA0A1Z1SYD564–243monomerMolecule count 120.15 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1295[3]0.0159736425–0.3633577228 1/AHas uncertainty columnMissing 030sasbdb/entries/k4/sasdek4/source/SASDEK4.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)5.4—Å
i0Guinier0.0040551e-061/cm
i0P(r)0.004053—1/cm
mwExperimental19.0—kDa
mwGuinier I(0)11.02.0kDa
mwPorod19.0—kDa
porod_volumePorod22200.0—ų
rgGuinier1.70.01Å
rgP(r)1.69—Å

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

Fit 1 · DAMMIN 5.3

χ²: 1.079CorMap p: 0.24638Unit: 1/A

Representative example of 1 of 16 dummy atom modelling optimisations.

ModelName / TypeSoftwareSymmetryModel MWPDB DeclarationSource file
1—dummyDAMFILT 5.0P116.086—Model Image

Fit 2 · CRYSOL 2.8.3

χ²: 1.12CorMap p: 0.017618Unit: 1/A
ModelName / TypeSoftwareSymmetryModel MWPDB DeclarationSource file
1—atomicPDB (Protein Data Bank) P119.724YX8Not available locally; open RCSB PDBModel Image
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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 name10mM HEPES, 150mM NaClBuffer concentration—
pH7.4Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2018-04-05Storage / measurement temperature4.0 / 10.0
Exposure time1.0Frames38
Wavelength0.1033Sample-to-detector distance3.33
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineAustralian Synchrotron / SAXS/WAXS · Melbourne, Australia
q range0.16 – 3.634Sample 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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full_entry_zip:source record and ZIP contents (6 items)
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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:182 field values
Field pathRaw value
codeSASDEK4
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleEngineered 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.titleEngineered 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_listFurlong EJ, Kurth F, Premkumar L, Whitten AE, Martin JL
project.publication.journalActa Crystallogr D Struct Biol
project.publication.doi10.1107/S2059798319000081
project.publication.pmid30950400
project.publication.published_date2019 Mar 1
project.statusreleased
project.submitted_date2018-09-18
project.released_date2019-03-29
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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_nameC-terminal catalytic domain of Suppressor of Copper Sensitivity C protein
experiment.sample.molecule[0].short_namePmScsCΔN
experiment.sample.molecule[0].sequenceSNAQFRQALASEHDALYNDAASPRIGAKDAKLVLVSFTDYNCPYCKRFDPLLEKITEQYPDVAVIIKPLPFKGESSAKASQAVLSVWKEDPKAFLALHQRLMQKKTMLDNASIEDAMKSTNTSKIKLTDDSLKTLQNNLELSRKLGIQGTPATVIGDTILPGAVDYDQLEIIVKEQLAKVKK
experiment.sample.molecule[0].organismProteus mirabilis
experiment.sample.molecule[0].uniprot_codeA0A1Z1SYD5
experiment.sample.molecule[0].uniprot_range_first64
experiment.sample.molecule[0].uniprot_range_last243
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMKKTLSVLVISSLLFGANVQAAALNAAQEKEVRALVRDTLVSNPEILEEAIMALQTKKAD EQQAQFRQALASEHDALYNDAASPRIGAKDAKLVLVSFTDYNCPYCKRFDPLLEKITEQY PDVAVIIKPLPFKGESSAKASQAVLSVWKEDPKAFLALHQRLMQKKTMLDNASIEDAMKS TNTSKIKLTDDSLKTLQNNLELSRKLGIQGTPATVIGDTILPGAVDYDQLEIIVKEQLAK VKK
experiment.sample.molecule[0].mw20.15
experiment.sample.molecule[0].total_mw20.15
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.name10mM 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.ph7.4
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameC-terminal catalytic domain of Suppressor of Copper Sensitivity C protein (ScsC)
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.date2018-04-05
experiment.storage_temperature4.0
experiment.cell_temperature10.0
experiment.exposure_time1.0
experiment.number_of_frames38
experiment.wavelength0.1033
experiment.sample_detector_distance3.33
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experiment.flow_ratenull
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experiment.seccolumnnull
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fits[1].p_value0.017618
fits[1].fit_residual_plotnull
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fits[1].description
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version4.6
i0_calibration_standardnull
descriptionnull
experiment_descriptionX-ray synchrotron radiation scattering data from solutions of the C-terminal catalytic domain 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 SAXS data displayed this entry was derived from a 0.50 mg/ml sample. The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted.
tags[]
intensity_unit1/cm
experimental_mw19.0
experimental_mw_errornull
guinier_i0_mw11.0
guinier_i0_mw_error2.0
porod_mw19.0
porod_mw_errornull
pddf_i00.004053
pddf_i0_errornull
guinier_i00.004055
guinier_i0_error1e-06
pddf_rg1.69
pddf_rg_errornull
guinier_rg1.7
guinier_rg_error0.01
pddf_dmax5.4
pddf_dmax_errornull
porod_volume22200.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first1
guinier_point_last52
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDEK4_datloglog_img.png
symmetrynull
last_modified2020-06-15T11:37:11.282615+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDEK4
statussuccess
started_at2026-08-11T16:25:16.687044+00:00
finished_at2026-08-11T16:25:25.450757+00:00
source_last_modified2020-06-15T11:37:11.282615+02:00
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View the complete summary.json source
{
  "code": "SASDEK4",
  "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.",
    "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.",
      "author_list": "Furlong EJ, Kurth F, Premkumar L, Whitten AE, Martin JL",
      "journal": "Acta Crystallogr D Struct Biol",
      "doi": "10.1107/S2059798319000081",
      "pmid": "30950400",
      "published_date": "2019 Mar 1"
    },
    "status": "released",
    "submitted_date": "2018-09-18",
    "released_date": "2019-03-29"
  },
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      },
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      "country": "Australia",
      "beamline_name": "SAXS/WAXS",
      "beam_geometry": "Point",
      "type_of_source": "X-ray synchrotron",
      "point_source": true,
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    },
    "sample": {
      "molecule": [
        {
          "long_name": "C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein",
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          "sequence": "SNAQFRQALASEHDALYNDAASPRIGAKDAKLVLVSFTDYNCPYCKRFDPLLEKITEQYPDVAVIIKPLPFKGESSAKASQAVLSVWKEDPKAFLALHQRLMQKKTMLDNASIEDAMKSTNTSKIKLTDDSLKTLQNNLELSRKLGIQGTPATVIGDTILPGAVDYDQLEIIVKEQLAKVKK",
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View the complete manifest.json source
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