SASDC48

ScsC-ScsBalpha complex

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2020-06-15T11:36:42.269791+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · ScsC-ScsBalpha complex

Concentration0.56 – 4.5 Buffer / pH10mM HEPES, 150mM NaCl / 7.5
Experimental temperature10.0 Facility / beamlineAustralian Synchrotron / SAXS/WAXS
Wavelength0.1033 nmExposure1.0 s × 13

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
DsbA-like protein
View sequence
SNAALNAAQEKEVRALVRDTLVSNPEILEEAIMALQTKKADEQQAQFRQALASEHDALYNDAASPRIGAKDAKLVLVSFTDYNCPYCKRFDPLLEKITEQYPDVAVIIKPLPFKGESSAKASQAVLSVWKEDPKAFLALHQRLMQKKTMLDNASIEDAMKSTNTSKIKLTDDSLKTLQNNLELSRKLGIQGTPATVIGDTILPGAVDYDQLEIIVKEQLAKVKK
proteinProteus mirabilisC2LPE222–243trimerMolecule count 324.768 kDa
Putative metal resistance protein
View sequence
MHHHHHHSSGVDLGTENLYFQSNADTGWLTMPDNDHAQVRATADKSSTGDVKILLEVQLAPGWKTYWRSPGEGGVAPEINWTQSVSDMIWHWPSPSAFDVAGIHTQGYDKEVVFPIELKSVDSDNLNGVLTLSTCSNVCILTDYSLNLDLNEPAPADFEWQYNQAMAKVPVTSGLISAVSSDYRNSQLTLSLQREQGDWHQPNIYLDPPQGMLYGIPQLTAKGDHLSVTVDVTDDWGDAAGDITGKALSFVVTDDGYSRQVNDTIGQGDSASLPTADS
proteinProteus mirabilisB4EV2022–275monomerMolecule count 130.343 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1372[3]0.010537851–0.29986023 1/AHas uncertainty columnMissing 010sasbdb/entries/48/sasdc48/source/SASDC48.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)11.53.0Å
i0Guinier0.040570.000121/cm
i0P(r)0.040260.00011/cm
mwExperimental95.0—kDa
mwGuinier I(0)95.05.0kDa
mwPorod119.0—kDa
porod_volumePorod145.0—ų
rgGuinier3.920.02Å
rgP(r)3.870.01Å

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 name10mM HEPES, 150mM NaClBuffer concentration—
pH7.5Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2016-11-02Storage / measurement temperature4.0 / 10.0
Exposure time1.0Frames13
Wavelength0.1033Sample-to-detector distance2.68
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineAustralian Synchrotron / SAXS/WAXS · Melbourne, Australia
q range0.105 – 2.999Sample 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

CategoryFileStatusSizeChecksumDownload and View
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pddfsasbdb/entries/48/sasdc48/source/SASDC48.outdownloaded321634a8547854c04a364de741ab87b24e5887d70a97915e121ce62bb3d4ac5e21889DownloadView source fileSource site
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summarysasbdb/entries/48/sasdc48/source/summary.jsondownloaded9636292803372ae36f00be23c5dcfbd4cf8f9f1be1748fa081ad35dd71dfa34ecbe3DownloadView source fileSource site
curve:source record
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full_entry_zip:source record and ZIP contents (6 items)
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pddf:source record
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sascif:source record
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summary:source record
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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:173 field values
Field pathRaw value
codeSASDC48
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleDisulfide isomerase activity of the dynamic, trimeric <b><i>Proteus mirabilis</i></b> ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB.
project.publication.titleDisulfide isomerase activity of the dynamic, trimeric <b><i>Proteus mirabilis</i></b> ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB.
project.publication.author_listFurlong EJ, Choudhury HG, Kurth F, Duff AP, Whitten AE, Martin JL
project.publication.journalJ Biol Chem
project.publication.doi10.1074/jbc.RA118.001860
project.publication.pmid29491145
project.publication.published_date2018 Apr 20
project.statusreleased
project.submitted_date2017-10-05
project.released_date2018-02-21
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDC48.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDC48.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDC48_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDC48_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDC48_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDC48_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDC48.sascif
experiment.instrument.detector.typeDectris
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 protein
experiment.sample.molecule[0].short_nameScsC
experiment.sample.molecule[0].sequenceSNAALNAAQEKEVRALVRDTLVSNPEILEEAIMALQTKKADEQQAQFRQALASEHDALYNDAASPRIGAKDAKLVLVSFTDYNCPYCKRFDPLLEKITEQYPDVAVIIKPLPFKGESSAKASQAVLSVWKEDPKAFLALHQRLMQKKTMLDNASIEDAMKSTNTSKIKLTDDSLKTLQNNLELSRKLGIQGTPATVIGDTILPGAVDYDQLEIIVKEQLAKVKK
experiment.sample.molecule[0].organismProteus mirabilis
experiment.sample.molecule[0].uniprot_codeC2LPE2
experiment.sample.molecule[0].uniprot_range_first22
experiment.sample.molecule[0].uniprot_range_last243
experiment.sample.molecule[0].oligomerizationtrimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequencenull
experiment.sample.molecule[0].mw24.768
experiment.sample.molecule[0].total_mw74.304
experiment.sample.molecule[0].number_molecules3
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.molecule[1].long_namePutative metal resistance protein
experiment.sample.molecule[1].short_nameScsB
experiment.sample.molecule[1].sequenceMHHHHHHSSGVDLGTENLYFQSNADTGWLTMPDNDHAQVRATADKSSTGDVKILLEVQLAPGWKTYWRSPGEGGVAPEINWTQSVSDMIWHWPSPSAFDVAGIHTQGYDKEVVFPIELKSVDSDNLNGVLTLSTCSNVCILTDYSLNLDLNEPAPADFEWQYNQAMAKVPVTSGLISAVSSDYRNSQLTLSLQREQGDWHQPNIYLDPPQGMLYGIPQLTAKGDHLSVTVDVTDDWGDAAGDITGKALSFVVTDDGYSRQVNDTIGQGDSASLPTADS
experiment.sample.molecule[1].organismProteus mirabilis
experiment.sample.molecule[1].uniprot_codeB4EV20
experiment.sample.molecule[1].uniprot_range_first22
experiment.sample.molecule[1].uniprot_range_last275
experiment.sample.molecule[1].oligomerizationmonomer
experiment.sample.molecule[1].molecular_typeprotein
experiment.sample.molecule[1].uniprot_sequenceMVRSFLIALMLMLFSLSSLAADTGWLTMPDNDHAQVRATADKSSTGDVKILLEVQLAPGW KTYWRSPGEGGVAPEINWTQSVSDMIWHWPSPSAFDVAGIHTQGYDKEVVFPIELKSVDS DNLNGVLTLSTCSNVCILTDYSLNLDLNEPAPADFEWQYNQAMAKVPVTSGLISAVSSDY RNSQLTLSLQREQGDWHQPNIYLDPPQGMLYGIPQLTAKGDHLSVTVDVTDDWGDAAGDI TGKALSFVVTDDGYSRQVNDTIGQGDSASLPTADSGVGLWSILAFALLGGLILNLMPCVL PVLAMKLGSILHIEKRDTGAIRKQFSVSVVGILVSFWALALFMTVLRYSQEAIGWGIQFQ SPWFIGFMVLITAIFTANLFGLFELRLSSNMNTKIATAGGQGYSRHFWEGAFATLLATPC SAPFLGTAVAYALIAPLSELWLIFTALGLGMSLPWIMVAMFPSIAKVLPKPGKWMNRLRV VLGFMMLLSCIWLITLLIPHFGIGIVAAIFVAIALILLFAIAKHYGKKTLFASMVITLIL GGTSYLFIAQPDTQTLAGQDHVNWQPLSEEAIHQALAENKRVFIDVTADWCVTCKANKYN VLLRDDVQKALSEPDVVALRGDWTKPSEQITQFLKQRGQVAVPFNQIYGPCNKEGEILPP LLNKDLMLTILSEAKGAQ
experiment.sample.molecule[1].mw30.343
experiment.sample.molecule[1].total_mw30.343
experiment.sample.molecule[1].number_molecules1
experiment.sample.molecule[1].complex_stateFalse
experiment.sample.molecule[1].deuterationnull
experiment.sample.molecule[1].molecule_sourcebiological
experiment.sample.molecule[1].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.ph7.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameScsC-ScsBalpha complex
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.date2016-11-02
experiment.storage_temperature4.0
experiment.cell_temperature10.0
experiment.exposure_time1.0
experiment.number_of_frames13
experiment.wavelength0.1033
experiment.sample_detector_distance2.68
experiment.concentration_min0.56
experiment.concentration_max4.5
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.105
experiment.s_max2.999
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[0].models[0].model_plothttps://www.sasbdb.org/media/pdb_file/images/SASDC48_fit1_model1_img.png
fits[0].models[0].softwareSASREF
fits[0].models[0].pdb_link[]
fits[0].models[0].model_titlenull
fits[0].models[0].type_of_modelatomic
fits[0].models[0].software_version7.d
fits[0].models[0].model_datahttps://www.sasbdb.org/media/pdb_file/SASDC48_fit1_model1.pdb
fits[0].models[0].model_mw99.99
fits[0].models[0].bead_radius1.9
fits[0].models[0].loghttps://www.sasbdb.org/media/log_files/run1_ZoMbNC2.log
fits[0].models[0].symmetryP1
fits[0].models[0].commentOverall symmetry is P1, but the ScsC component possesses P3 symmetry
fits[0].models[0].user111
fits[0].fit_unit1/A
fits[0].fit_plothttps://www.sasbdb.org/media/fitting_files/scattering_plots/SASDC48_fit1_fit_img.png
fits[0].softwareSASREF
fits[0].chi_square_value1.7956
fits[0].p_value0.0
fits[0].fit_residual_plotSASDC48_fit1_fitresiduals_img.png
fits[0].fit_datahttps://www.sasbdb.org/media/fitting_files/SASDC48_fit1.fit
fits[0].fit_loghttps://www.sasbdb.org/media/fitting_files/log_files/run1_ZTJcGes.log
fits[0].software_version7.d
fits[0].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version4.6
i0_calibration_standardnull
descriptionnull
experiment_descriptionX-ray synchrotron radiation scattering data from solutions of Suppressor of Copper Sensitivity C protein (ScsC) complexed with the alpha domain of the Suppressor of Copper Sensitivity B protein from Proteus mirabilis in 10 mM HEPES 100mM NaCl, pH 7.5 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). Thirteen successive 1 second frames were collected across solute concentrations of 0.56-4.50 mg/ml. The SAXS data displayed this entry was derived from a 0.56 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. Small-angle neutron scattering data with contrast variation were also collected on the QUOKKA instrument at the Australian Nuclear Science and Technology Organisation at a solute concentration of ~5.0 mg/ml. A rigid-body model was co-refined against the SAXS and SANS data using using SASREF (v 7.d), and this model is shown, together with the X-ray data and correspond fit. Details of the SANS data collection, corresponding fits, and additional analysis are contained in a downloadable zip archive.
tags[]
intensity_unit1/cm
experimental_mw95.0
experimental_mw_errornull
guinier_i0_mw95.0
guinier_i0_mw_error5.0
porod_mw119.0
porod_mw_errornull
pddf_i00.04026
pddf_i0_error0.0001
guinier_i00.04057
guinier_i0_error0.00012
pddf_rg3.87
pddf_rg_error0.01
guinier_rg3.92
guinier_rg_error0.02
pddf_dmax11.5
pddf_dmax_error3.0
porod_volume145.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first1
guinier_point_last30
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDC48_datloglog_img.png
symmetrynull
last_modified2020-06-15T11:36:42.269791+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDC48
statussuccess
started_at2026-08-11T15:45:23.446957+00:00
finished_at2026-08-11T15:45:32.777217+00:00
source_last_modified2020-06-15T11:36:42.269791+02:00
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View the complete summary.json source
{
  "code": "SASDC48",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Disulfide isomerase activity of the dynamic, trimeric <b><i>Proteus mirabilis</i></b> ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB.",
    "publication": {
      "title": "Disulfide isomerase activity of the dynamic, trimeric <b><i>Proteus mirabilis</i></b> ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB.",
      "author_list": "Furlong EJ, Choudhury HG, Kurth F, Duff AP, Whitten AE, Martin JL",
      "journal": "J Biol Chem",
      "doi": "10.1074/jbc.RA118.001860",
      "pmid": "29491145",
      "published_date": "2018 Apr 20"
    },
    "status": "released",
    "submitted_date": "2017-10-05",
    "released_date": "2018-02-21"
  },
  "pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDC48.out",
  "intensities_data": "https://www.sasbdb.org/media/intensities_files/SASDC48.dat",
  "intensities_log_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDC48_dat_img.png",
  "intensities_kratky_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDC48_kratky_img.png",
  "pddf_plot": "https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDC48_pofr_img.png",
  "intensities_guinier_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDC48_guinier_img.png",
  "sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDC48.sascif",
  "experiment": {
    "instrument": {
      "detector": {
        "type": "Dectris",
        "name": "Pilatus 1M",
        "resolution": 172.0
      },
      "name": "Australian  Synchrotron",
      "city": "Melbourne",
      "country": "Australia",
      "beamline_name": "SAXS/WAXS",
      "beam_geometry": "Point",
      "type_of_source": "X-ray synchrotron",
      "point_source": true,
      "line_collimation": null,
      "sample_path_length": null,
      "line_collimation_slitlength": null,
      "line_collimation_integrationwidth": null,
      "xray_energy": null,
      "beam_profile_ah": null,
      "beam_profile_al": null
    },
    "sample": {
      "molecule": [
        {
          "long_name": "DsbA-like protein",
          "short_name": "ScsC",
          "sequence": "SNAALNAAQEKEVRALVRDTLVSNPEILEEAIMALQTKKADEQQAQFRQALASEHDALYNDAASPRIGAKDAKLVLVSFTDYNCPYCKRFDPLLEKITEQYPDVAVIIKPLPFKGESSAKASQAVLSVWKEDPKAFLALHQRLMQKKTMLDNASIEDAMKSTNTSKIKLTDDSLKTLQNNLELSRKLGIQGTPATVIGDTILPGAVDYDQLEIIVKEQLAKVKK",
          "organism": "Proteus mirabilis",
          "uniprot_code": "C2LPE2",
          "uniprot_range_first": 22,
          "uniprot_range_last": 243,
          "oligomerization": "trimer",
          "molecular_type": "protein",
          "uniprot_sequence": null,
          "mw": 24.768,
          "total_mw": 74.304,
          "number_molecules": 3,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        },
        {
          "long_name": "Putative metal resistance protein",
          "short_name": "ScsB",
          "sequence": "MHHHHHHSSGVDLGTENLYFQSNADTGWLTMPDNDHAQVRATADKSSTGDVKILLEVQLAPGWKTYWRSPGEGGVAPEINWTQSVSDMIWHWPSPSAFDVAGIHTQGYDKEVVFPIELKSVDSDNLNGVLTLSTCSNVCILTDYSLNLDLNEPAPADFEWQYNQAMAKVPVTSGLISAVSSDYRNSQLTLSLQREQGDWHQPNIYLDPPQGMLYGIPQLTAKGDHLSVTVDVTDDWGDAAGDITGKALSFVVTDDGYSRQVNDTIGQGDSASLPTADS",
          "organism": "Proteus mirabilis",
          "uniprot_code": "B4EV20",
          "uniprot_range_first": 22,
          "uniprot_range_last": 275,
          "oligomerization": "monomer",
          "molecular_type": "protein",
          "uniprot_sequence": "MVRSFLIALMLMLFSLSSLAADTGWLTMPDNDHAQVRATADKSSTGDVKILLEVQLAPGW\nKTYWRSPGEGGVAPEINWTQSVSDMIWHWPSPSAFDVAGIHTQGYDKEVVFPIELKSVDS\nDNLNGVLTLSTCSNVCILTDYSLNLDLNEPAPADFEWQYNQAMAKVPVTSGLISAVSSDY\nRNSQLTLSLQREQGDWHQPNIYLDPPQGMLYGIPQLTAKGDHLSVTVDVTDDWGDAAGDI\nTGKALSFVVTDDGYSRQVNDTIGQGDSASLPTADSGVGLWSILAFALLGGLILNLMPCVL\nPVLAMKLGSILHIEKRDTGAIRKQFSVSVVGILVSFWALALFMTVLRYSQEAIGWGIQFQ\nSPWFIGFMVLITAIFTANLFGLFELRLSSNMNTKIATAGGQGYSRHFWEGAFATLLATPC\nSAPFLGTAVAYALIAPLSELWLIFTALGLGMSLPWIMVAMFPSIAKVLPKPGKWMNRLRV\nVLGFMMLLSCIWLITLLIPHFGIGIVAAIFVAIALILLFAIAKHYGKKTLFASMVITLIL\nGGTSYLFIAQPDTQTLAGQDHVNWQPLSEEAIHQALAENKRVFIDVTADWCVTCKANKYN\nVLLRDDVQKALSEPDVVALRGDWTKPSEQITQFLKQRGQVAVPFNQIYGPCNKEGEILPP\nLLNKDLMLTILSEAKGAQ",
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          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        }
      ],
      "buffer": {
        "name": "10mM HEPES, 150mM NaCl",
        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 7.5,
        "deuteration": null
      },
      "purity_method": null,
      "name": "ScsC-ScsBalpha complex",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": "ANSTO",
            "address": "Kirrawee DC, NSW 2232, Australia",
            "full_name": "Australian Nuclear Science and Technology Organisation",
            "webpage": ""
          }
        ],
        "contributor_name": "Andrew",
        "contributor_surname": "Whitten",
        "orcid": null
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2016-11-02",
    "storage_temperature": 4.0,
    "cell_temperature": 10.0,
    "exposure_time": 1.0,
    "number_of_frames": 13,
    "wavelength": 0.1033,
    "sample_detector_distance": 2.68,
    "concentration_min": 0.56,
    "concentration_max": 4.5,
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    "flow_rate": null,
    "s_min": 0.105,
    "s_max": 2.999,
    "total_exposure_time": null,
    "seccolumn": null
  },
  "fits": [
    {
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        {
          "model_plot": "https://www.sasbdb.org/media/pdb_file/images/SASDC48_fit1_model1_img.png",
          "software": "SASREF",
          "pdb_link": [],
          "model_title": null,
          "type_of_model": "atomic",
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          "log": "https://www.sasbdb.org/media/log_files/run1_ZoMbNC2.log",
          "symmetry": "P1",
          "comment": "Overall symmetry is P1, but the ScsC component possesses P3 symmetry",
          "user": 111
        }
      ],
      "fit_unit": "1/A",
      "fit_plot": "https://www.sasbdb.org/media/fitting_files/scattering_plots/SASDC48_fit1_fit_img.png",
      "software": "SASREF",
      "chi_square_value": 1.7956,
      "p_value": 0.0,
      "fit_residual_plot": "SASDC48_fit1_fitresiduals_img.png",
      "fit_data": "https://www.sasbdb.org/media/fitting_files/SASDC48_fit1.fit",
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  "i0_calibration_standard": null,
  "description": null,
  "experiment_description": "X-ray synchrotron radiation scattering data from solutions of Suppressor of Copper Sensitivity C protein (ScsC) complexed with the alpha domain of the Suppressor of Copper Sensitivity B protein from Proteus mirabilis in 10 mM HEPES 100mM NaCl, pH 7.5 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). Thirteen successive 1 second frames were collected across solute concentrations of 0.56-4.50 mg/ml. The SAXS data displayed this entry was derived from a 0.56 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. Small-angle neutron scattering data with contrast variation were also collected on the QUOKKA instrument at the Australian Nuclear Science and Technology Organisation at a solute concentration of ~5.0 mg/ml. A rigid-body model was co-refined against the SAXS and SANS data using using SASREF (v 7.d), and this model is shown, together with the X-ray data and correspond fit. Details of the SANS data collection, corresponding fits, and additional analysis are contained in a downloadable zip archive.",
  "tags": [],
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  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDC48_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2020-06-15T11:36:42.269791+02:00",
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}
View the complete manifest.json source
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