SASDFK3

Splicing factor, proline- and glutamine-rich (SFPQ)

Data type: SASBDB experimental data Status: Published Curve type: SEC-SAS Last updated: 2019-12-06T13:07:15.624532+01:00

CORAL was used to compare the scattering profile against the two PDB models of SFPQ in either P212121 or C2221 crystallographic space groups (CRYSOL fits to the data are shown; Coral models and fits are included in the full entry zip archive).

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Splicing factor, proline- and glutamine-rich (SFPQ)

Concentration— – 5.0 Buffer / pH20 mM Tris-HCl, 250 mM NaCl, 5% (v/v) glycerol / 7.5
Experimental temperature25.0 Facility / beamlineAustralian Synchrotron / SAXS/WAXS
Wavelength0.10332 nmExposure1.0 s × 4

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Splicing factor, proline- and glutamine-rich
View sequence
GAMEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLL
proteinHomo sapiensP23246276–535dimerMolecule count 230.049 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1881[3]0.00878155–0.351796 1/AHas uncertainty columnMissing 040sasbdb/entries/k3/sasdfk3/source/SASDFK3.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)8.2—Å
i0Guinier0.059110.00016arbitrary
i0P(r)0.058710.00016arbitrary
mwExperimental60.58—kDa
mwGuinier I(0)60.58—kDa
mwPorod57.0—kDa
porod_volumePorod91.0—ų
rgGuinier2.770.01Å
rgP(r)2.7310.008Å

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 name20 mM Tris-HCl, 250 mM NaCl, 5% (v/v) glycerolBuffer concentration—
pH7.5Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2018-04-19Storage / measurement temperature— / 25.0
Exposure time1.0Frames4
Wavelength0.10332Sample-to-detector distance2.68
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineAustralian Synchrotron / SAXS/WAXS · Melbourne, Australia
q range0.088 – 3.518Sample 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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All source fields (unfiltered)

Every source field is expanded here, including empty values, list members and fields already shown above.

summary.json:185 field values
Field pathRaw value
codeSASDFK3
statusPublished
type_of_curveSEC-SAS
angular_unit1/A
project.titleA new crystal structure and small-angle X-ray scattering analysis of the homodimer of human SFPQ.
project.publication.titleA new crystal structure and small-angle X-ray scattering analysis of the homodimer of human SFPQ.
project.publication.author_listHewage TW, Caria S, Lee M
project.publication.journalActa Crystallogr F Struct Biol Commun
project.publication.doi10.1107/S2053230X19006599
project.publication.pmid31204691
project.publication.published_date2019 Jun 1
project.statusreleased
project.submitted_date2019-02-28
project.released_date2019-05-27
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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_nameSplicing factor, proline- and glutamine-rich
experiment.sample.molecule[0].short_nameSFPQ
experiment.sample.molecule[0].sequenceGAMEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFG FIKLESRALAEIAKAELDDTPMRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFG PIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDD EDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDA KDKLESEMEDAYHEHQANLL
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeP23246
experiment.sample.molecule[0].uniprot_range_first276
experiment.sample.molecule[0].uniprot_range_last535
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].mw30.049
experiment.sample.molecule[0].total_mw60.098
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_descriptionnull
experiment.sample.buffer.name20 mM Tris-HCl, 250 mM NaCl, 5% (v/v) glycerol
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
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experiment.sample.purity_methodnull
experiment.sample.nameSplicing factor, proline- and glutamine-rich (SFPQ)
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_nameSofia
experiment.contributor[0].contributor_surnameCaria
experiment.contributor[0].orcid
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2018-04-19
experiment.storage_temperaturenull
experiment.cell_temperature25.0
experiment.exposure_time1.0
experiment.number_of_frames4
experiment.wavelength0.10332
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fits[0].p_value8.7e-05
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fits[1].softwareCRYSOL
fits[1].chi_square_value2.256
fits[1].p_value0.011216
fits[1].fit_residual_plotSFPQ_C2221_dimer_fitresiduals_img.png
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fits[1].description
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5
i0_calibration_standardnull
descriptionCORAL was used to compare the scattering profile against the two PDB models of SFPQ in either P212121 or C2221 crystallographic space groups (CRYSOL fits to the data are shown; Coral models and fits are included in the full entry zip archive).
experiment_descriptionSynchrotron SAXS data from solutions of SFPQ in 20 mM Tris-HCl, 250 mM NaCl, 5% (v/v) glycerol, pH 7.5 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus 2-1M detector at a sample-detector distance of 2.68 m and at a wavelength of λ = 0.10332 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Data was collected in an in-line SEC-SAXS experimental setup coupled to a co-flow sample sheath flow environment run at a fractional sample flow rate of 0.5 mL/min at 25°C. The protein complex was analysed after size exclusion chromatography using a Superdex 200 5/150 column (45μl of sample injected at 5mg/ml). The low angle data collected were obtained from a single scattering curve obtained by selecting data from the peak with highest intensity and consistent Rg. Given that coflow was used for the measurements, the I(0) here presented was corrected by a factor 2.05 (original I(0) is 0.059). The data presented corresponds to a two standard errors.
tags[]
intensity_unitarbitrary
experimental_mw60.58
experimental_mw_errornull
guinier_i0_mw60.58
guinier_i0_mw_errornull
porod_mw57.0
porod_mw_errornull
pddf_i00.05871
pddf_i0_error0.00016
guinier_i00.05911
guinier_i0_error0.00016
pddf_rg2.731
pddf_rg_error0.008
guinier_rg2.77
guinier_rg_error0.01
pddf_dmax8.2
pddf_dmax_errornull
porod_volume91.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first8
guinier_point_last106
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDFK3_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDFK3
statussuccess
started_at2026-08-11T14:02:02.322045+00:00
finished_at2026-08-11T14:02:11.983476+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDFK3",
  "status": "Published",
  "type_of_curve": "SEC-SAS",
  "angular_unit": "1/A",
  "project": {
    "title": "A new crystal structure and small-angle X-ray scattering analysis of the homodimer of human SFPQ.",
    "publication": {
      "title": "A new crystal structure and small-angle X-ray scattering analysis of the homodimer of human SFPQ.",
      "author_list": "Hewage TW, Caria S, Lee M",
      "journal": "Acta Crystallogr F Struct Biol Commun",
      "doi": "10.1107/S2053230X19006599",
      "pmid": "31204691",
      "published_date": "2019 Jun 1"
    },
    "status": "released",
    "submitted_date": "2019-02-28",
    "released_date": "2019-05-27"
  },
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          {
            "short_name": "ANSTO",
            "address": "Kirrawee DC, NSW 2232, Australia",
            "full_name": "Australian Nuclear Science and Technology Organisation",
            "webpage": ""
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  "last_modified": "2019-12-06T13:07:15.624532+01:00",
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View the complete manifest.json source
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