SASDEQ7

Filamin A Ig-like domains 3-5 (FLNa3-5)

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

SAXS data describing the Filamin A Ig-like domains 3-5 in solution. The experiment was done to enable comparison with the corresponding P637Q mutated fragment (SASDEP7).

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Filamin A Ig-like domains 3-5 (FLNa3-5)

Concentration1.0 – 4.0 Buffer / pH20 mM Tris, 100 mM NaCl, 1 mM DTT / 8.0
Experimental temperature20.0 Facility / beamlineESRF / BM29
Wavelength0.1 nmExposure1.0 s × 10

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Filamin A Ig-like domains 3-5
View sequence
>FLNA3-5CNPSACRAVGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGFEYYPMVPGTYIVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAG
proteinHomo sapiensP21333478–766monomerMolecule count 130.76 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11037[3]0.060004–4.93699 1/nmHas uncertainty columnMissing 02sasbdb/entries/q7/sasdeq7/source/SASDEQ7.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)7.340.5nm
i0Guinier25.640.1arbitrary
i0P(r)25.64—arbitrary
mwExperimental24.7—kDa
porod_volumePorod39.0—nm³
rgGuinier2.190.1nm
rgP(r)2.2—nm

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, 100 mM NaCl, 1 mM DTTBuffer concentration—
pH8.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2017-02-10Storage / measurement temperature— / 20.0
Exposure time1.0Frames10
Wavelength0.1Sample-to-detector distance2.9
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineESRF / BM29 · Grenoble, France
q range0.06 – 4.937Sample 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:159 field values
Field pathRaw value
codeSASDEQ7
statusPublished
type_of_curveMerged
angular_unit1/nm
project.titleNon-syndromic Mitral Valve Dysplasia Mutation Changes the Force Resilience and Interaction of Human Filamin A.
project.publication.titleNon-syndromic Mitral Valve Dysplasia Mutation Changes the Force Resilience and Interaction of Human Filamin A.
project.publication.author_listHaataja TJK, Bernardi RC, Lecointe S, Capoulade R, Merot J, Pentikäinen U
project.publication.journalStructure
project.publication.doi10.1016/j.str.2018.09.007
project.publication.pmid30344108
project.publication.published_date2018 Oct 9
project.statusreleased
project.submitted_date2018-11-12
project.released_date2018-11-12
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDEQ7.out
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intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDEQ7_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDEQ7_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDEQ7_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDEQ7.sascif
experiment.instrument.detector.typeDectris
experiment.instrument.detector.namePilatus 1M
experiment.instrument.detector.resolution172.0
experiment.instrument.nameESRF
experiment.instrument.cityGrenoble
experiment.instrument.countryFrance
experiment.instrument.beamline_nameBM29
experiment.instrument.beam_geometry
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_nameFilamin A Ig-like domains 3-5
experiment.sample.molecule[0].short_nameFLNa3-5
experiment.sample.molecule[0].sequence>FLNa3-5 CNPSACRAVGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGFEYYPMVPGTYIVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAG
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeP21333
experiment.sample.molecule[0].uniprot_range_first478
experiment.sample.molecule[0].uniprot_range_last766
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMSSSHSRAGQSAAGAAPGGGVDTRDAEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCV SKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIK LVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWDEEEDEEAKKQTPKQRLLGWIQNKL PQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQ VITPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPLRPKLNPKKARAYGPGIEPTGNMVKK RAEFTVETRSAGQGEVLVYVEDPAGHQEEAKVTANNDKNRTFSVWYVPEVTGTHKVTVLF AGQHIAKSPFEVYVDKSQGDASKVTAQGPGLEPSGNIANKTTYFEIFTAGAGTGEVEVVI QDPMGQKGTVEPQLEARGDSTYRCSYQPTMEGVHTVHVTFAGVPIPRSPYTVTVGQACNP SACRAVGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGF EYYPMVPGTYIVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGVVGKSADFVVE AIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFM ADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVE ALVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVA KTGLKAHEPTYFTVDCAEAGQGDVSIGIKCAPGVVGPAEADIDFDIIRNDNDTFTVKYTP RGAGSYTIMVLFADQATPTSPIRVKVEPSHDASKVKAEGPGLSRTGVELGKPTHFTVNAK AAGKGKLDVQFSGLTKGDAVRDVDIIDHHDNTYTVKYTPVQQGPVGVNVTYGGDPIPKSP FSVAVSPSLDLSKIKVSGLGEKVDVGKDQEFTVKSKGAGGQGKVASKIVGPSGAAVPCKV EPGLGADNSVVRFLPREEGPYEVEVTYDGVPVPGSPFPLEAVAPTKPSKVKAFGPGLQGG SAGSPARFTIDTKGAGTGGLGLTVEGPCEAQLECLDNGDGTCSVSYVPTEPGDYNINILF ADTHIPGSPFKAHVVPCFDASKVKCSGPGLERATAGEVGQFQVDCSSAGSAELTIEICSE AGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGGQPVPNFPSKLQVEPAVDTSGVQC YGPGIEGQGVFREATTEFSVDARALTQTGGPHVKARVANPSGNLTETYVQDRGDGMYKVE YTPYEEGLHSVDVTYDGSPVPSSPFQVPVTEGCDPSRVRVHGPGIQSGTTNKPNKFTVET RGAGTGGLGLAVEGPSEAKMSCMDNKDGSCSVEYIPYEAGTYSLNVTYGGHQVPGSPFKV PVHDVTDASKVKCSGPGLSPGMVRANLPQSFQVDTSKAGVAPLQVKVQGPKGLVEPVDVV DNADGTQTVNYVPSREGPYSISVLYGDEEVPRSPFKVKVLPTHDASKVKASGPGLNTTGV PASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILI KYGGDEIPFSPYRVRAVPTGDASKCTVTVSIGGHGLGAGIGPTIQIGEETVITVDTKAAG KGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFGGEHVPNSPFQVTA LAGDQPSVQPPLRSQQLAPQYTYAQGGQQTWAPERPLVGVNGLDVTSLRPFDLVIPFTIK KGEITGEVRMPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSPLQFYV DYVNCGHVTAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPSKAEISCTDNQDGTC SVSYLPVLPGDYSILVKYNEQHVPGSPFTARVTGDDSMRMSHLKVGSAADIPINISETDL SLLTATVVPPSGREEPCLLKRLRNGHVGISFVPKETGEHLVHVKKNGQHVASSPIPVVIS QSEIGDASRVRVSGQGLHEGHTFEPAEFIIDTRDAGYGGLSLSIEGPSKVDINTEDLEDG TCRVTYCPTEPGNYIINIKFADQHVPGSPFSVKVTGEGRVKESITRRRRAPSVANVGSHC DLSLKIPEISIQDMTAQVTSPSGKTHEAEIVEGENHTYCIRFVPAEMGTHTVSVKYKGQH VPGSPFQFTVGPLGEGGAHKVRAGGPGLERAEAGVPAEFSIWTREAGAGGLAIAVEGPSK AEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNEEHIPDSPFVVPVASPSGDARRLTVSSL QESGLKVNQPASFAVSLNGAKGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVY LIDVKFNGTHIPGSPFKIRVGEPGHGGDPGLVSAYGAGLEGGVTGNPAEFVVNTSNAGAG ALSVTIDGPSKVKMDCQECPEGYRVTYTPMAPGSYLISIKYGGPYHIGGSPFKAKVTGPR LVSNHSLHETSSVFVDSLTKATCAPQHGAPGPGPADASKVVAKGLGLSKAYVGQKSSFTV DCSKAGNNMLLVGVHGPRTPCEEILVKHVGSRLYSVSYLLKDKGEYTLVVKWGDEHIPGS PYRVVVP
experiment.sample.molecule[0].mw30.76
experiment.sample.molecule[0].total_mw30.76
experiment.sample.molecule[0].number_molecules1
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, 100 mM NaCl, 1 mM 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.ph8.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameFilamin A Ig-like domains 3-5 (FLNa3-5)
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].addressJyväskylän, Finland
experiment.contributor[0].affiliation[0].full_nameUniversity of Jyväskylä
experiment.contributor[0].affiliation[0].webpagehttps://www.jyu.fi
experiment.contributor[0].contributor_nameTatu
experiment.contributor[0].contributor_surnameHaataja
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2017-02-10
experiment.storage_temperaturenull
experiment.cell_temperature20.0
experiment.exposure_time1.0
experiment.number_of_frames10
experiment.wavelength0.1
experiment.sample_detector_distance2.9
experiment.concentration_min1.0
experiment.concentration_max4.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.06
experiment.s_max4.937
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].softwarePDB (Protein Data Bank)
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fits[0].models[0].commentnull
fits[0].models[0].user251
fits[0].fit_unit1/A
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fits[0].softwareCRYSOL
fits[0].chi_square_value1.001
fits[0].p_value0.0
fits[0].fit_residual_plotfit4columns1920_fitresiduals_img.png
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fits[0].fit_lognull
fits[0].software_versionnull
fits[0].description
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version4.6
i0_calibration_standardnull
descriptionSAXS data describing the Filamin A Ig-like domains 3-5 in solution. The experiment was done to enable comparison with the corresponding P637Q mutated fragment (SASDEP7).
experiment_descriptionSynchrotron SAXS data from solutions of Filamin A Ig-like domains 3-5 in 20 mM Tris, 100 mM NaCl, 1 mM DTT, pH 8 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 4 mg/ml were measured at 20°C. 10 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.
tags[]
intensity_unitarbitrary
experimental_mw24.7
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i025.64
pddf_i0_errornull
guinier_i025.64
guinier_i0_error0.1
pddf_rg2.2
pddf_rg_errornull
guinier_rg2.19
guinier_rg_error0.1
pddf_dmax7.34
pddf_dmax_error0.5
porod_volume39.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first8
guinier_point_last114
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDEQ7_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDEQ7
statussuccess
started_at2026-08-11T16:27:12.174165+00:00
finished_at2026-08-11T16:27:20.697810+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDEQ7",
  "status": "Published",
  "type_of_curve": "Merged",
  "angular_unit": "1/nm",
  "project": {
    "title": "Non-syndromic Mitral Valve Dysplasia Mutation Changes the Force Resilience and Interaction of Human Filamin A.",
    "publication": {
      "title": "Non-syndromic Mitral Valve Dysplasia Mutation Changes the Force Resilience and Interaction of Human Filamin A.",
      "author_list": "Haataja TJK, Bernardi RC, Lecointe S, Capoulade R, Merot J, Pentikäinen U",
      "journal": "Structure",
      "doi": "10.1016/j.str.2018.09.007",
      "pmid": "30344108",
      "published_date": "2018 Oct 9"
    },
    "status": "released",
    "submitted_date": "2018-11-12",
    "released_date": "2018-11-12"
  },
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      "line_collimation_integrationwidth": null,
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          "molecule_description": null
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        "concentration_unit": null,
        "comment": null,
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        "concentration": null,
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        "deuteration": null
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      "purity_method": null,
      "name": "Filamin A Ig-like domains 3-5 (FLNa3-5)",
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      "absorbption": null,
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    "contributor": [
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        "affiliation": [
          {
            "short_name": null,
            "address": "Jyväskylän, Finland",
            "full_name": "University of Jyväskylä",
            "webpage": "https://www.jyu.fi"
          }
        ],
        "contributor_name": "Tatu",
        "contributor_surname": "Haataja",
        "orcid": null
      }
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    "concentration_method": null,
    "concentration_unit": null,
    "date": "2017-02-10",
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  "description": "SAXS data describing the Filamin A Ig-like domains 3-5 in solution. The experiment was done to enable comparison with the corresponding P637Q mutated  fragment (SASDEP7).",
  "experiment_description": "Synchrotron SAXS data from solutions of Filamin A Ig-like domains 3-5 in 20 mM Tris, 100 mM NaCl, 1 mM DTT, pH 8 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 4 mg/ml were measured at 20°C. 10 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.",
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  "symmetry": null,
  "last_modified": "2019-12-06T13:07:15.624532+01:00",
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}
View the complete manifest.json source
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