SASDV67

Human Splicing Factor Proline/Glutamine rich SFPQ1 dimer with C-terminal truncation (delta599-707)

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2025-07-03T11:05:27.067416+02:00

SFPQ as a dimer truncated to remove the C-terminal Intrinsically Disordered Region (IDR). Experiment carried out at the SAXS/WAXS beamline with protein at 5mg/ml in 500mM KNO3, 20mM HEPES (pH 7.4), 5% glycerol, 1mM DTT. This data is part of 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/Glutamine rich SFPQ1 dimer with C-terminal truncation (delta599-707)

Concentration— – 5.0 Buffer / pH500mM KNO3, 20mM HEPES, 5% glycerol, 1mM DTT / 7.4
Experimental temperature25.0 Facility / beamlineAustralian Synchrotron / SAXS/WAXS
Wavelength0.10781 nmExposure1.0 s × 400

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Splicing Factor Proline/Glutamine rich (1-598)
View sequence
GAMSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPIPPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPGVGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQAGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGEPRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLMRRQEELRRMEELHNQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYS
proteinHomo sapiensP232461–598dimerMolecule count 265.148 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11402[3]0.004706911–0.4919686 1/AHas uncertainty columnMissing 0300sasbdb/entries/67/sasdv67/source/SASDV67.dat
▼

2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)34.3—Å
i0Guinier0.0335721—arbitrary
i0P(r)0.03449—arbitrary
mwExperimental161.077—kDa
mwPorod331.0—kDa
porod_volumePorod400.0—ų
rgGuinier7.5550.39Å
rgP(r)8.37—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 name500mM KNO3, 20mM HEPES, 5% glycerol, 1mM DTTBuffer concentration—
pH7.4Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2023-03-13Storage / measurement temperature25.0 / 25.0
Exposure time1.0Frames400
Wavelength0.10781Sample-to-detector distance3.0
SourceX-ray synchrotronDetectorPilatus3 S 2M
Facility / beamlineAustralian Synchrotron / SAXS/WAXS · Melbourne, Australia
q range0.047 – 4.92Sample 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 (2 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:134 field values
Field pathRaw value
codeSASDV67
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
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experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus3 S 2M
experiment.instrument.detector.resolution172.0
experiment.instrument.nameAustralian Synchrotron
experiment.instrument.cityMelbourne
experiment.instrument.countryAustralia
experiment.instrument.beamline_nameSAXS/WAXS
experiment.instrument.beam_geometrynull
experiment.instrument.type_of_sourceX-ray synchrotron
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/Glutamine rich (1-598)
experiment.sample.molecule[0].short_nameSFPQ1-598
experiment.sample.molecule[0].sequenceGAMSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPIPPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPGVGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQAGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGEPRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLMRRQEELRRMEELHNQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYS
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeP23246
experiment.sample.molecule[0].uniprot_range_first1
experiment.sample.molecule[0].uniprot_range_last598
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].mw65.148
experiment.sample.molecule[0].total_mw130.296
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_description
experiment.sample.buffer.name500mM KNO3, 20mM HEPES, 5% glycerol, 1mM DTT
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.nameHuman Splicing Factor Proline/Glutamine rich SFPQ1 dimer with C-terminal truncation (delta599-707)
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.date2023-03-13
experiment.storage_temperature25.0
experiment.cell_temperature25.0
experiment.exposure_time1.0
experiment.number_of_frames400
experiment.wavelength0.10781
experiment.sample_detector_distance3.0
experiment.concentration_minnull
experiment.concentration_max5.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.047
experiment.s_max4.92
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionSFPQ as a dimer truncated to remove the C-terminal Intrinsically Disordered Region (IDR). Experiment carried out at the SAXS/WAXS beamline with protein at 5mg/ml in 500mM KNO3, 20mM HEPES (pH 7.4), 5% glycerol, 1mM DTT. This data is part of the manuscript ' Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation '.
experiment_descriptionnull
tags[]
intensity_unitarbitrary
experimental_mw161.077
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw331.0
porod_mw_errornull
pddf_i00.03449
pddf_i0_errornull
guinier_i00.0335721
guinier_i0_errornull
pddf_rg8.37
pddf_rg_errornull
guinier_rg7.555
guinier_rg_error0.39
pddf_dmax34.3
pddf_dmax_errornull
porod_volume400.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first2
guinier_point_last36
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDV67_datloglog_img.png
symmetrynull
last_modified2025-07-03T11:05:27.067416+02:00
bragg_peak[]
manifest.json:34 field values
Field pathRaw value
codeSASDV67
statussuccess
started_at2026-08-11T15:23:15.750352+00:00
finished_at2026-08-11T15:23:22.931750+00:00
source_last_modified2025-07-03T11:05:27.067416+02:00
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View the complete summary.json source
{
  "code": "SASDV67",
  "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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          "long_name": "Splicing Factor Proline/Glutamine rich (1-598)",
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          "uniprot_range_first": 1,
          "uniprot_range_last": 598,
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          "mw": 65.148,
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          "molecule_description": ""
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View the complete manifest.json source
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