SASDV57

Full-length SFPQ in high salt buffer

Data type: SASBDB experimental data Status: Published Curve type: SEC-SAS Last updated: 2025-07-03T11:05:26.761664+02:00

A dimer of full-length SFPQ at 4.2mg/ml in 500mM KNO3, 20mM HEPES (pH 7.4), 5% glycerol, 1mM DTT. Measurement was taken at the Australian Synchrotron SAXS/WAXS beamline and 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 · Full-length SFPQ in high salt buffer

Concentration— – 4.2 Buffer / pH500mM KNO3, 20mM HEPES, 5% glycerol, 1mM DTT / 7.4
Experimental temperature25.0 Facility / beamlineAustralian Synchrotron / SAXS/WAXS
Wavelength0.10781 nmExposure1.0 s × 700

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
11515[3]0.005061195–0.5704002 1/AHas uncertainty columnMissing 0420sasbdb/entries/57/sasdv57/source/SASDV57.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)42.5—Å
i0Guinier0.0259164—1/cm
i0P(r)0.02728—1/cm
mwExperimental200.46—kDa
mwPorod380.0—kDa
porod_volumePorod485.0—ų
rgGuinier7.9351.807Å
rgP(r)9.5—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 date2022-10-22Storage / measurement temperature25.0 / 25.0
Exposure time1.0Frames700
Wavelength0.10781Sample-to-detector distance2.79
SourceX-ray synchrotronDetectorPilatus3 S 2M
Facility / beamlineAustralian Synchrotron / SAXS/WAXS · Melbourne, Australia
q range0.051 – 5.704Sample volume / flow rate60.0 / 0.4

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:128 field values
Field pathRaw value
codeSASDV57
statusPublished
type_of_curveSEC-SAS
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/SASDV57.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDV57.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDV57_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDV57_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDV57_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDV57_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDV57.sascif
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- 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.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.nameFull-length SFPQ in high salt buffer
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[]
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2022-10-22
experiment.storage_temperature25.0
experiment.cell_temperature25.0
experiment.exposure_time1.0
experiment.number_of_frames700
experiment.wavelength0.10781
experiment.sample_detector_distance2.79
experiment.concentration_minnull
experiment.concentration_max4.2
experiment.sample_volume60.0
experiment.flow_rate0.4
experiment.s_min0.051
experiment.s_max5.704
experiment.total_exposure_timenull
experiment.seccolumn2
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionA dimer of full-length SFPQ at 4.2mg/ml in 500mM KNO3, 20mM HEPES (pH 7.4), 5% glycerol, 1mM DTT. Measurement was taken at the Australian Synchrotron SAXS/WAXS beamline and is part of the manuscript ' Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation '.
experiment_descriptionSynchrotron SAXS data from solutions of Dimeric full-length human Splicing factor, proline- and glutamine-rich (SFPQ) in 500mM KNO3, 20mM HEPES, 5% glycerol, 1mM DTT, pH 7.4 were collected on the SAXS/WAXS beam line at the Australian Synchrotron storage ring (Melbourne, Australia) using a Pilatus3 S 2M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.10781 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 60.00 μl sample at 4.2 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 25°C. 450 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. A dimer of full-length SFPQ at 4.2mg/ml in 500mM KNO3, 20mM HEPES (pH 7.4), 5% glycerol, 1mM DTT. Measurement was taken at the Australian Synchrotron SAXS/WAXS beamline and is part of the manuscript ' Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation '.
tags[]
intensity_unit1/cm
experimental_mw200.46
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw380.0
porod_mw_errornull
pddf_i00.02728
pddf_i0_errornull
guinier_i00.0259164
guinier_i0_errornull
pddf_rg9.5
pddf_rg_errornull
guinier_rg7.935
guinier_rg_error1.807
pddf_dmax42.5
pddf_dmax_errornull
porod_volume485.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first3
guinier_point_last31
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDV57_datloglog_img.png
symmetrynull
last_modified2025-07-03T11:05:26.761664+02:00
bragg_peak[]
manifest.json:34 field values
Field pathRaw value
codeSASDV57
statussuccess
started_at2026-08-11T15:22:42.467699+00:00
finished_at2026-08-11T15:22:49.872967+00:00
source_last_modified2025-07-03T11:05:26.761664+02:00
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View the complete summary.json source
{
  "code": "SASDV57",
  "status": "Published",
  "type_of_curve": "SEC-SAS",
  "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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      "city": "Melbourne",
      "country": "Australia",
      "beamline_name": "SAXS/WAXS",
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          "long_name": "Splicing factor, proline- and glutamine-rich",
          "short_name": "SFPQ cysteine dimer",
          "sequence": "GAMSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPIPPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPGVGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQAGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGEPRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLMRRQEELRRMEELHNQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRMGYMDPRERDMRMGGGGAMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGSDMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF",
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          "uniprot_code": "P23246",
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          "uniprot_range_last": 707,
          "oligomerization": "dimer",
          "molecular_type": "protein",
          "uniprot_sequence": "MSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPI\nPPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPG\nVGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQ\nAGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGE\nPRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLF\nVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGR\nQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFAS\nKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRF\nAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLM\nRRQEELRRMEELHNQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRM\nGYMDPRERDMRMGGGGAMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGS\nDMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF",
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          "number_molecules": 2,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": "R542C mutation causes monomers of SFPQ to dimerise via the coiled-coil domain (Lee et al, 2015)"
        }
      ],
      "buffer": {
        "name": "500mM KNO3, 20mM HEPES, 5% glycerol, 1mM DTT",
        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 7.4,
        "deuteration": null
      },
      "purity_method": null,
      "name": "Full-length SFPQ in high salt buffer",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2022-10-22",
    "storage_temperature": 25.0,
    "cell_temperature": 25.0,
    "exposure_time": 1.0,
    "number_of_frames": 700,
    "wavelength": 0.10781,
    "sample_detector_distance": 2.79,
    "concentration_min": null,
    "concentration_max": 4.2,
    "sample_volume": 60.0,
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    "s_min": 0.051,
    "s_max": 5.704,
    "total_exposure_time": null,
    "seccolumn": 2
  },
  "fits": [],
  "estimated_volume_method": null,
  "pddf_software": "ATSAS GNOM",
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  "i0_calibration_standard": null,
  "description": "A dimer of full-length SFPQ at 4.2mg/ml in 500mM KNO3, 20mM HEPES (pH 7.4), 5% glycerol, 1mM DTT. \r\n\r\nMeasurement was taken at the Australian Synchrotron SAXS/WAXS beamline and is part of the manuscript ' Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation '.",
  "experiment_description": "Synchrotron SAXS data from solutions of Dimeric full-length human Splicing factor, proline- and glutamine-rich (SFPQ) in 500mM KNO3, 20mM HEPES, 5% glycerol, 1mM DTT, pH 7.4 were collected on the SAXS/WAXS beam line at the Australian Synchrotron storage ring (Melbourne, Australia) using a Pilatus3 S 2M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.10781 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 60.00 μl sample at 4.2 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 25°C. 450 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. A dimer of full-length SFPQ at 4.2mg/ml in 500mM KNO3, 20mM HEPES (pH 7.4), 5% glycerol, 1mM DTT. Measurement was taken at the Australian Synchrotron SAXS/WAXS beamline and is part of the manuscript ' Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation '.",
  "tags": [],
  "intensity_unit": "1/cm",
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  "guinier_i0": 0.0259164,
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  "porod_volume": 485.0,
  "porod_volume_error": null,
  "estimated_volume": null,
  "estimated_volume_error": null,
  "guinier_point_first": 3,
  "guinier_point_last": 31,
  "pddf_point_first": null,
  "pddf_point_last": null,
  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDV57_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2025-07-03T11:05:26.761664+02:00",
  "bragg_peak": []
}
View the complete manifest.json source
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