SASDV59

Human Splicing factor, proline- and glutamine-rich protein 5% SFPQ and 95% dSFPQ at a D2O matchpoint of 95%

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2025-07-03T11:05:27.816508+02:00

SANS experiment indicating dimer partner exchange between deuterated and protiated monomers of full-length SFPQ. Contrast-matching has ensured signal is coming from protiated monomers of full-length SFPQ. Additional details are available in the manuscript: Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Human Splicing factor, proline- and glutamine-rich protein 5% SFPQ and 95% dSFPQ at a D2O matchpoint of 95%

Concentration— – — Buffer / pH150 mM KCl, 0.075% glycerol, 20 mM HEPES, 0.5 mM DTT, / 7.4
Experimental temperature25.0 Facility / beamlineAustralian Centre for Neutron Scattering (ANSTO) / Quokka - Small Angle Neutron Scattering
Wavelength0.6 nmExposure— s × —

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Splicing factor, proline- and glutamine-rich
View sequence
GAMSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPIPPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPGVGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQAGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGEPRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLMRRQEELRRMEELHNQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRMGYMDPRERDMRMGGGGAMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGSDMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF
proteinHomo sapiensP23246214–707dimerMolecule count 276.277 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1218[3]0.00815–0.4352 1/AHas uncertainty columnMissing 02sasbdb/entries/59/sasdv59/source/SASDV59.dat
▼

2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)22.0—Å
i0Guinier0.0285187—arbitrary
i0P(r)0.02926—arbitrary
mwExperimental41.25—kDa
mwPorod113.0—kDa
porod_volumePorod181.0—ų
rgGuinier6.1090.418Å
rgP(r)6.64—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

This entry has no source fit record.

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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 name150 mM KCl, 0.075% glycerol, 20 mM HEPES, 0.5 mM DTT,Buffer concentration—
pH7.4Additives—
Buffer descriptionSANS contrast matching buffer
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2023-01-20Storage / measurement temperature25.0 / 25.0
Exposure time—Frames—
Wavelength0.6Sample-to-detector distance1.3
Sourceneutron sourceDetectorORDELA/21000N
Facility / beamlineAustralian Centre for Neutron Scattering (ANSTO) / Quokka - Small Angle Neutron Scattering · Lucas Heights, Sydney, Australia
q range0.082 – 4.352Sample 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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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:134 field values
Field pathRaw value
codeSASDV59
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleStructural dynamics of IDR interactions in human SFPQ and implications for liquid–liquid phase separation
project.publication.titleStructural dynamics of IDR interactions in human SFPQ and implications for liquid–liquid phase separation
project.publication.author_listKoning H, Lai V, Sethi A, Chakraborty S, Ang C, Fox A, Duff A, Whitten A, Marshall A, Bond C
project.publication.journalActa Crystallographica Section D Structural Biology
project.publication.doi10.1107/S2059798325005303
project.publication.pmidnull
project.publication.published_date2025 Jun 27
project.statusreleased
project.submitted_date2024-09-18
project.released_date2025-06-29
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDV59.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDV59.dat
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intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDV59_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDV59.sascif
experiment.instrument.detector.typenull
experiment.instrument.detector.nameORDELA/21000N
experiment.instrument.detector.resolution5.1
experiment.instrument.nameAustralian Centre for Neutron Scattering (ANSTO)
experiment.instrument.cityLucas Heights, Sydney
experiment.instrument.countryAustralia
experiment.instrument.beamline_nameQuokka - Small Angle Neutron Scattering
experiment.instrument.beam_geometrynull
experiment.instrument.type_of_sourceneutron source
experiment.instrument.point_sourcenull
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_nameSplicing factor, proline- and glutamine-rich
experiment.sample.molecule[0].short_nameSFPQ cysteine dimer
experiment.sample.molecule[0].sequenceGAMSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPIPPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPGVGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQAGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGEPRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLMRRQEELRRMEELHNQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRMGYMDPRERDMRMGGGGAMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGSDMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeP23246
experiment.sample.molecule[0].uniprot_range_first214
experiment.sample.molecule[0].uniprot_range_last707
experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPI PPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPG VGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQ AGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGE PRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLF VGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGR QLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFAS KPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRF AQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLM RRQEELRRMEELHNQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRM GYMDPRERDMRMGGGGAMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGS DMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF
experiment.sample.molecule[0].mw76.277
experiment.sample.molecule[0].total_mw152.554
experiment.sample.molecule[0].number_molecules2
experiment.sample.molecule[0].complex_stateFalse
experiment.sample.molecule[0].deuterationnull
experiment.sample.molecule[0].molecule_sourcebiological
experiment.sample.molecule[0].molecule_descriptionR542C mutation causes monomers of SFPQ to dimerise via the coiled-coil domain (Lee et al, 2015)
experiment.sample.buffer.name150 mM KCl, 0.075% glycerol, 20 mM HEPES, 0.5 mM DTT,
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentSANS contrast matching buffer
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.4
experiment.sample.buffer.deuteration95.0
experiment.sample.purity_methodnull
experiment.sample.nameHuman Splicing factor, proline- and glutamine-rich protein 5% SFPQ and 95% dSFPQ at a D2O matchpoint of 95%
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_namenull
experiment.contributor[0].affiliation[0].addressnull
experiment.contributor[0].affiliation[0].full_nameThe University of Western Australia
experiment.contributor[0].affiliation[0].webpagenull
experiment.contributor[0].contributor_nameHeidar
experiment.contributor[0].contributor_surnameKoning
experiment.contributor[0].orcid
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2023-01-20
experiment.storage_temperature25.0
experiment.cell_temperature25.0
experiment.exposure_timenull
experiment.number_of_framesnull
experiment.wavelength0.6
experiment.sample_detector_distance1.3
experiment.concentration_minnull
experiment.concentration_maxnull
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.082
experiment.s_max4.352
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionSANS experiment indicating dimer partner exchange between deuterated and protiated monomers of full-length SFPQ. Contrast-matching has ensured signal is coming from protiated monomers of full-length SFPQ. Additional details are available in the manuscript: Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation.
experiment_descriptionnull
tags[]
intensity_unitarbitrary
experimental_mw41.25
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw113.0
porod_mw_errornull
pddf_i00.02926
pddf_i0_errornull
guinier_i00.0285187
guinier_i0_errornull
pddf_rg6.64
pddf_rg_errornull
guinier_rg6.109
guinier_rg_error0.418
pddf_dmax22.0
pddf_dmax_errornull
porod_volume181.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first7
guinier_point_last19
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDV59_datloglog_img.png
symmetrynull
last_modified2025-07-03T11:05:27.816508+02:00
bragg_peak[]
manifest.json:34 field values
Field pathRaw value
codeSASDV59
statussuccess
started_at2026-08-11T16:06:50.778354+00:00
finished_at2026-08-11T16:06:57.721373+00:00
source_last_modified2025-07-03T11:05:27.816508+02:00
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View the complete summary.json source
{
  "code": "SASDV59",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Structural dynamics of IDR interactions in human SFPQ and implications for liquid–liquid phase separation",
    "publication": {
      "title": "Structural dynamics of IDR interactions in human SFPQ and implications for liquid–liquid phase separation",
      "author_list": "Koning H, Lai V, Sethi A, Chakraborty S, Ang C, Fox A, Duff A, Whitten A, Marshall A, Bond C",
      "journal": "Acta Crystallographica Section D Structural Biology",
      "doi": "10.1107/S2059798325005303",
      "pmid": null,
      "published_date": "2025 Jun 27"
    },
    "status": "released",
    "submitted_date": "2024-09-18",
    "released_date": "2025-06-29"
  },
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      },
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      "country": "Australia",
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      "beam_geometry": null,
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      "point_source": null,
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    "sample": {
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          "long_name": "Splicing factor, proline- and glutamine-rich",
          "short_name": "SFPQ cysteine dimer",
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          "uniprot_range_last": 707,
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          "molecular_type": "protein",
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        "concentration": null,
        "pka": null,
        "ph": 7.4,
        "deuteration": 95.0
      },
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      "name": "Human Splicing factor, proline- and glutamine-rich protein 5% SFPQ and 95% dSFPQ at a D2O matchpoint of 95%",
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      "contrast": null,
      "specific_vol": null,
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    "contributor": [
      {
        "affiliation": [
          {
            "short_name": null,
            "address": null,
            "full_name": "The University of Western Australia",
            "webpage": null
          }
        ],
        "contributor_name": "Heidar",
        "contributor_surname": "Koning",
        "orcid": ""
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2023-01-20",
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    "exposure_time": null,
    "number_of_frames": null,
    "wavelength": 0.6,
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    "concentration_min": null,
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  "description": "SANS experiment indicating dimer partner exchange between deuterated and protiated monomers of full-length SFPQ. Contrast-matching has ensured signal is coming from protiated monomers of full-length SFPQ.\r\n\r\nAdditional details are available in the manuscript: Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation.",
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  "tags": [],
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  "pddf_point_last": null,
  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDV59_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2025-07-03T11:05:27.816508+02:00",
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}
View the complete manifest.json source
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