SASDVB6

Pentraxin-3 truncation mutant lacking the first 24 amino acids per mature promoter

Data type: SASBDB experimental data Status: Published Curve type: SEC-SAS Last updated: 2025-07-27T15:24:02.558358+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Pentraxin-3 truncation mutant lacking the first 24 amino acids per mature promoter

Concentration— – 8.5 Buffer / pH137 mM NaCl, 2.7 mM KCl, 10 mM phosphate buffer / 7.4
Experimental temperature20.0 Facility / beamlineDiamond Light Source / B21
Wavelength0.095 nmExposure1.0 s × 620

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Pentraxin-related protein PTX3 (N-terminal deletion mutant)
View sequence
ELEDPTPCACGQEHSEWDKLFIMLENSQMRERMLLQATDDVLRGELQRLREELGRLAESLARPCAPGAPAEARLTSALDELLQATRDAGRRLARMEGAEAQRPEEAGRALAAVLEELRQTRADLHAVQGWAARSWLPAGCETAILFPMRSKKIFGSVHPVRPMRLESFSACIWVKATDVLNKTILFSYGTKRNPYEIQLYLSYQSIVFVVGGEENKLVAEAMVSLGRWTHLCGTWNSEEGLTSLWVNGELAATTVEMATGHIVPEGGILQIGQEKNGCCVGGGFDETLAFSGRLTGFNIWDSVLSNEEIRETGGAESCHIRGNIVGWGVTEIQPHGGAQYVS
proteinHomo sapiensP2602242–381octamerMolecule count 837.584 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11584[4]0.00602004–0.214248 1/AHas uncertainty columnMissing 012sasbdb/entries/b6/sasdvb6/source/SASDVB6.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)40.0—Å
i0Guinier0.260703—arbitrary
i0P(r)26574.02—arbitrary
mwExperimental331.621—kDa
mwGuinier I(0)384.929—kDa
porod_volumePorod647.0—ų
rgGuinier8.3720.64Å
rgP(r)9.52—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

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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 name137 mM NaCl, 2.7 mM KCl, 10 mM phosphate bufferBuffer concentration—
pH7.4Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2020-02-06Storage / measurement temperature4.0 / 20.0
Exposure time1.0Frames620
Wavelength0.095Sample-to-detector distance2.7
SourceX-ray synchrotronDetectorPilatus 2M
Facility / beamlineDiamond Light Source / B21 · Didcot, UK
q range0.06 – 2.142Sample volume / flow rate45.0 / 0.08

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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All source fields (unfiltered)

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

summary.json:156 field values
Field pathRaw value
codeSASDVB6
statusPublished
type_of_curveSEC-SAS
angular_unit1/A
project.titleThe structural organisation of pentraxin-3 and its interactions with heavy chains of inter-α-inhibitor regulate crosslinking of the hyaluronan matrix
project.publication.titleThe structural organisation of pentraxin-3 and its interactions with heavy chains of inter-α-inhibitor regulate crosslinking of the hyaluronan matrix
project.publication.author_listShah A, Zhang X, Snee M, Lockhart-Cairns M, Levy C, Jowitt T, Birchenough H, Dean L, Collins R, Dodd R, Roberts A, Enghild J, Mantovani A, Fontana J, Baldock C, Inforzato A, Richter R, Day A
project.publication.journalMatrix Biology
project.publication.doi10.1016/j.matbio.2025.01.002
project.publication.pmidnull
project.publication.published_date2025 Apr
project.statusreleased
project.submitted_date2024-08-19
project.released_date2025-07-27
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDVB6.dat
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDVB6.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDVB6_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDVB6_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDVB6_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDVB6_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDVB6.sascif
experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus 2M
experiment.instrument.detector.resolutionnull
experiment.instrument.nameDiamond Light Source
experiment.instrument.cityDidcot
experiment.instrument.countryUK
experiment.instrument.beamline_nameB21
experiment.instrument.beam_geometry1 x 5 mm
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_namePentraxin-related protein PTX3 (N-terminal deletion mutant)
experiment.sample.molecule[0].short_nameΔ1-24 PTX3
experiment.sample.molecule[0].sequenceELEDPTPCACGQEHSEWDKLFIMLENSQMRERMLLQATDDVLRGELQRLREELGRLAESL ARPCAPGAPAEARLTSALDELLQATRDAGRRLARMEGAEAQRPEEAGRALAAVLEELRQT RADLHAVQGWAARSWLPAGCETAILFPMRSKKIFGSVHPVRPMRLESFSACIWVKATDVL NKTILFSYGTKRNPYEIQLYLSYQSIVFVVGGEENKLVAEAMVSLGRWTHLCGTWNSEEG LTSLWVNGELAATTVEMATGHIVPEGGILQIGQEKNGCCVGGGFDETLAFSGRLTGFNIW DSVLSNEEIRETGGAESCHIRGNIVGWGVTEIQPHGGAQYVS
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeP26022
experiment.sample.molecule[0].uniprot_range_first42
experiment.sample.molecule[0].uniprot_range_last381
experiment.sample.molecule[0].oligomerizationoctamer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMHLLAILFCALWSAVLAENSDDYDLMYVNLDNEIDNGLHPTEDPTPCACGQEHSEWDKLF IMLENSQMRERMLLQATDDVLRGELQRLREELGRLAESLARPCAPGAPAEARLTSALDEL LQATRDAGRRLARMEGAEAQRPEEAGRALAAVLEELRQTRADLHAVQGWAARSWLPAGCE TAILFPMRSKKIFGSVHPVRPMRLESFSACIWVKATDVLNKTILFSYGTKRNPYEIQLYL SYQSIVFVVGGEENKLVAEAMVSLGRWTHLCGTWNSEEGLTSLWVNGELAATTVEMATGH IVPEGGILQIGQEKNGCCVGGGFDETLAFSGRLTGFNIWDSVLSNEEIRETGGAESCHIR GNIVGWGVTEIQPHGGAQYVS
experiment.sample.molecule[0].mw37.584
experiment.sample.molecule[0].total_mw300.672
experiment.sample.molecule[0].number_molecules8
experiment.sample.molecule[0].complex_stateFalse
experiment.sample.molecule[0].deuterationnull
experiment.sample.molecule[0].molecule_sourcebiological
experiment.sample.molecule[0].molecule_descriptionΔ1-24 PTX3 was expressed in human embryonic kidney (HEK) Expi293F cells and is therefore glycosylated. The amino acid numbering of the deletion mutant (Δ1-24) refers to the amino acid numbering of the mature protein, i.e., after the signal sequence has been cleaved (and therefore this construct corresponds to the removal of amino acids 1-17 (signal sequence) and 18-41 (Δ1-24) from the UniProt P26022 reference sequence). A48 isoform. The protein construct used for SAXS also contains and additional two non-native amino acids at the N-terminus (EL).
experiment.sample.buffer.name137 mM NaCl, 2.7 mM KCl, 10 mM phosphate buffer
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.namePentraxin-3 truncation mutant lacking the first 24 amino acids per mature promoter
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].addressManchester, UK
experiment.contributor[0].affiliation[0].full_nameUniversity of Manchester
experiment.contributor[0].affiliation[0].webpagehttp://www.manchester.ac.uk/
experiment.contributor[0].contributor_nameAnokhi
experiment.contributor[0].contributor_surnameShah
experiment.contributor[0].orcidhttps://orcid.org/0000-0001-9818-5573
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2020-02-06
experiment.storage_temperature4.0
experiment.cell_temperature20.0
experiment.exposure_time1.0
experiment.number_of_frames620
experiment.wavelength0.095
experiment.sample_detector_distance2.7
experiment.concentration_minnull
experiment.concentration_max8.5
experiment.sample_volume45.0
experiment.flow_rate0.08
experiment.s_min0.06
experiment.s_max2.142
experiment.total_exposure_timenull
experiment.seccolumn59
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fits[0].models[0].softwareAllosMod
fits[0].models[0].pdb_link[]
fits[0].models[0].model_titlenull
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fits[0].models[0].model_mw323.0
fits[0].models[0].bead_radiusnull
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fits[0].models[0].commentnull
fits[0].models[0].user1107
fits[0].fit_unit1/A
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fits[0].softwareFoXS
fits[0].chi_square_value25.471879
fits[0].p_value0.0
fits[0].fit_residual_plotSASDVB6_fit1_fitresiduals_img.png
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fits[0].fit_lognull
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fits[0].description
estimated_volume_methodnull
pddf_softwareScÅtter
pddf_software_versionnull
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from solutions of Pentraxin-3 (N-terminal deletion mutant) in 137 mM NaCl, 2.7 mM KCl, 10 mM phosphate buffer, pH 7.4 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Pilatus 2M detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.095 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 45.00 μl sample at 8.5 mg/ml was injected at a 0.075 ml/min flow rate onto a Cytiva Superose 6 Increase 3.2/300 column at 20°C. 620 successive 1 second frames were collected throughout the entire SEC elution. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
tags[]
intensity_unitarbitrary
experimental_mw331.621
experimental_mw_errornull
guinier_i0_mw384.929
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i026574.02
pddf_i0_errornull
guinier_i00.260703
guinier_i0_errornull
pddf_rg9.52
pddf_rg_errornull
guinier_rg8.372
guinier_rg_error0.64
pddf_dmax40.0
pddf_dmax_errornull
porod_volume647.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first15
guinier_point_last55
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDVB6_datloglog_img.png
symmetrynull
last_modified2025-07-27T15:24:02.558358+02:00
bragg_peak[]
manifest.json:34 field values
Field pathRaw value
codeSASDVB6
statussuccess
started_at2026-08-11T15:06:01.802085+00:00
finished_at2026-08-11T15:06:10.734987+00:00
source_last_modified2025-07-27T15:24:02.558358+02:00
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View the complete summary.json source
{
  "code": "SASDVB6",
  "status": "Published",
  "type_of_curve": "SEC-SAS",
  "angular_unit": "1/A",
  "project": {
    "title": "The structural organisation of pentraxin-3 and its interactions with heavy chains of inter-α-inhibitor regulate crosslinking of the hyaluronan matrix",
    "publication": {
      "title": "The structural organisation of pentraxin-3 and its interactions with heavy chains of inter-α-inhibitor regulate crosslinking of the hyaluronan matrix",
      "author_list": "Shah A, Zhang X, Snee M, Lockhart-Cairns M, Levy C, Jowitt T, Birchenough H, Dean L, Collins R, Dodd R, Roberts A, Enghild J, Mantovani A, Fontana J, Baldock C, Inforzato A, Richter R, Day A",
      "journal": "Matrix Biology",
      "doi": "10.1016/j.matbio.2025.01.002",
      "pmid": null,
      "published_date": "2025 Apr"
    },
    "status": "released",
    "submitted_date": "2024-08-19",
    "released_date": "2025-07-27"
  },
  "pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDVB6.dat",
  "intensities_data": "https://www.sasbdb.org/media/intensities_files/SASDVB6.dat",
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  "sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDVB6.sascif",
  "experiment": {
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        "name": "Pilatus 2M",
        "resolution": null
      },
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      "city": "Didcot",
      "country": "UK",
      "beamline_name": "B21",
      "beam_geometry": "1 x 5 mm",
      "type_of_source": "X-ray synchrotron",
      "point_source": null,
      "line_collimation": null,
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    "sample": {
      "molecule": [
        {
          "long_name": "Pentraxin-related protein PTX3 (N-terminal deletion mutant)",
          "short_name": "Δ1-24 PTX3",
          "sequence": "ELEDPTPCACGQEHSEWDKLFIMLENSQMRERMLLQATDDVLRGELQRLREELGRLAESL         \r\nARPCAPGAPAEARLTSALDELLQATRDAGRRLARMEGAEAQRPEEAGRALAAVLEELRQT       \r\nRADLHAVQGWAARSWLPAGCETAILFPMRSKKIFGSVHPVRPMRLESFSACIWVKATDVL        \r\nNKTILFSYGTKRNPYEIQLYLSYQSIVFVVGGEENKLVAEAMVSLGRWTHLCGTWNSEEG        \r\nLTSLWVNGELAATTVEMATGHIVPEGGILQIGQEKNGCCVGGGFDETLAFSGRLTGFNIW \r\nDSVLSNEEIRETGGAESCHIRGNIVGWGVTEIQPHGGAQYVS",
          "organism": "Homo sapiens",
          "uniprot_code": "P26022",
          "uniprot_range_first": 42,
          "uniprot_range_last": 381,
          "oligomerization": "octamer",
          "molecular_type": "protein",
          "uniprot_sequence": "MHLLAILFCALWSAVLAENSDDYDLMYVNLDNEIDNGLHPTEDPTPCACGQEHSEWDKLF\nIMLENSQMRERMLLQATDDVLRGELQRLREELGRLAESLARPCAPGAPAEARLTSALDEL\nLQATRDAGRRLARMEGAEAQRPEEAGRALAAVLEELRQTRADLHAVQGWAARSWLPAGCE\nTAILFPMRSKKIFGSVHPVRPMRLESFSACIWVKATDVLNKTILFSYGTKRNPYEIQLYL\nSYQSIVFVVGGEENKLVAEAMVSLGRWTHLCGTWNSEEGLTSLWVNGELAATTVEMATGH\nIVPEGGILQIGQEKNGCCVGGGFDETLAFSGRLTGFNIWDSVLSNEEIRETGGAESCHIR\nGNIVGWGVTEIQPHGGAQYVS",
          "mw": 37.584,
          "total_mw": 300.672,
          "number_molecules": 8,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": "Δ1-24 PTX3 was expressed in human embryonic kidney (HEK) Expi293F cells and is therefore glycosylated. The amino acid numbering of the deletion mutant (Δ1-24) refers to the amino acid numbering of the mature protein, i.e., after the signal sequence has been cleaved (and therefore this construct corresponds to the removal of amino acids 1-17 (signal sequence) and 18-41 (Δ1-24) from the UniProt P26022 reference sequence). A48 isoform. The protein construct used for SAXS also contains and additional two non-native amino acids at the N-terminus (EL)."
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      ],
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        "name": "137 mM NaCl, 2.7 mM KCl, 10 mM phosphate buffer",
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      "name": "Pentraxin-3 truncation mutant lacking the first 24 amino acids per mature promoter",
      "ext_coefficient": null,
      "contrast": null,
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      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": null,
            "address": "Manchester, UK",
            "full_name": "University of Manchester",
            "webpage": "http://www.manchester.ac.uk/"
          }
        ],
        "contributor_name": "Anokhi",
        "contributor_surname": "Shah",
        "orcid": "https://orcid.org/0000-0001-9818-5573"
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2020-02-06",
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    "seccolumn": 59
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  "symmetry": null,
  "last_modified": "2025-07-27T15:24:02.558358+02:00",
  "bragg_peak": []
}
View the complete manifest.json source
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