SASDV56

Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to Ubiquitin at tau residue C317

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2025-04-10T13:15:30.028980+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Microtubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to Ubiquitin at tau residue C317

Concentration— – 3.0 Buffer / pH100 mM NaCl / 6.8
Experimental temperature20.0 Facility / beamlinePETRA III / EMBL P12
Wavelength0.123972 nmExposure0.05 s × 20

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Isoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A)
View sequence
MQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKAGSKDNIKHVPGGGSVQIVYCPVDLSCVTSKAGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE
proteinHomo sapiensP10636244–372monomerMolecule count 113.7 kDa
Polyubiquitin-B
View sequence
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC
proteinFukomys damarensisA0A091E2601–77monomerMolecule count 18.668 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11352[3]0.089688–3.99835 1/nmHas uncertainty columnMissing 010sasbdb/entries/56/sasdv56/source/SASDV56.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)13.3—nm
i0Guinier0.0489423—1/cm
i0P(r)0.0499—1/cm
mwExperimental20.66—kDa
mwPorod25.8—kDa
porod_volumePorod41.3—nm³
rgGuinier3.340.046nm
rgP(r)3.598—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 name100 mM NaClBuffer concentration—
pH6.8Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2023-03-17Storage / measurement temperature10.0 / 20.0
Exposure time0.05Frames20
Wavelength0.123972Sample-to-detector distance3.0
SourceX-ray synchrotronDetectorPilatus 6M
Facility / beamlinePETRA III / EMBL P12 · DESY; Hamburg, Germany
q range0.09 – 3.998Sample 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

CategoryFileStatusSizeChecksumDownload and View
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sascifsasbdb/entries/56/sasdv56/source/SASDV56.sascifnot_available——DownloadView source fileSource site
summarysasbdb/entries/56/sasdv56/source/summary.jsondownloaded10155af38e5eb3f024d2d289455356cc6b018a7e2f20af1eec944e9f6d113df391ddfDownloadView source fileSource site
curve:source record
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full_entry_zip:source record and ZIP contents (7 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:196 field values
Field pathRaw value
codeSASDV56
statusPublished
type_of_curveSingle concentration
angular_unit1/nm
project.titleConformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain.
project.publication.titleConformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain.
project.publication.author_listViola G, Trivellato D, Laitaoja M, Jänis J, Felli IC, D'Onofrio M, Mollica L, Giachin G, Assfalg M
project.publication.journalProc Natl Acad Sci U S A
project.publication.doi10.1073/pnas.2425831122
project.publication.pmid40198698
project.publication.published_date2025 Apr 15
project.statusreleased
project.submitted_date2024-08-13
project.released_date2025-03-21
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDV56.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDV56.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDV56_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDV56_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDV56_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDV56_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDV56.sascif
experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus 6M
experiment.instrument.detector.resolutionnull
experiment.instrument.namePETRA III
experiment.instrument.cityDESY; Hamburg
experiment.instrument.countryGermany
experiment.instrument.beamline_nameEMBL P12
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_nameIsoform Tau-F of Microtubule-associated protein tau (C291A, K311C, K317C, C322A)
experiment.sample.molecule[0].short_nametau4RD domain
experiment.sample.molecule[0].sequenceMQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKAGSKDNIKHV PGGGSVQIVYCPVDLSCVTSKAGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIE
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeP10636
experiment.sample.molecule[0].uniprot_range_first244
experiment.sample.molecule[0].uniprot_range_last372
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPG SETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAG HVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPK TPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAK SRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHV PGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNI THVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMV DSPQLATLADEVSASLAKQGL
experiment.sample.molecule[0].mw13.7
experiment.sample.molecule[0].total_mw13.7
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_descriptionTau4RD (Q244-E372 plus initial methionine) with C291A, C322A, K311C, K317C mutations referred to as tau4RDΔC(311/317C)
experiment.sample.molecule[1].long_namePolyubiquitin-B
experiment.sample.molecule[1].short_namenull
experiment.sample.molecule[1].sequenceMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPP DQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC
experiment.sample.molecule[1].organismFukomys damarensis
experiment.sample.molecule[1].uniprot_codeA0A091E260
experiment.sample.molecule[1].uniprot_range_first1
experiment.sample.molecule[1].uniprot_range_last77
experiment.sample.molecule[1].oligomerizationmonomer
experiment.sample.molecule[1].molecular_typeprotein
experiment.sample.molecule[1].uniprot_sequenceMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGGC
experiment.sample.molecule[1].mw8.668
experiment.sample.molecule[1].total_mw8.668
experiment.sample.molecule[1].number_molecules1
experiment.sample.molecule[1].complex_stateFalse
experiment.sample.molecule[1].deuterationnull
experiment.sample.molecule[1].molecule_sourcebiological
experiment.sample.molecule[1].molecule_descriptionThe semisynthetic ubiquitination reaction was performed without major modifications to the already outlined protocol. Briefly, Ub-SH was activated with 5,5′-dithiobis(2-nitrobenzoic acid) (DTNB) and incubated with each tau mutant in a 1:4 tau:Ub molar ratio. The desired proteoform was then purified through ion exchange chromatography exploiting a linear gradient of NaCl.
experiment.sample.buffer.name100 mM NaCl
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph6.8
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameMicrotubule-associated protein tau, lysine-rich four-repeat domain 4RD synthetically linked to Ubiquitin at tau residue C317
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_nameESRF
experiment.contributor[0].affiliation[0].addressGrenoble, France
experiment.contributor[0].affiliation[0].full_nameEuropean Synchrotron Radiation Facility
experiment.contributor[0].affiliation[0].webpagehttp://www.esrf.eu/
experiment.contributor[0].contributor_nameGabriele
experiment.contributor[0].contributor_surnameGiachin
experiment.contributor[0].orcidhttps://orcid.org/0000-0001-7550-0307
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2023-03-17
experiment.storage_temperature10.0
experiment.cell_temperature20.0
experiment.exposure_time0.05
experiment.number_of_frames20
experiment.wavelength0.123972
experiment.sample_detector_distance3.0
experiment.concentration_minnull
experiment.concentration_max3.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.09
experiment.s_max3.998
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].softwareEOM/RANCH
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fits[0].models[0].model_mw10.58
fits[0].models[0].bead_radius1.9
fits[0].models[0].lognull
fits[0].models[0].symmetrynull
fits[0].models[0].commentnull
fits[0].models[0].user388
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fits[0].softwareEOM/GAJOE
fits[0].chi_square_value1.045
fits[0].p_value0.28
fits[0].fit_residual_plotSASDV56_fit1_fitresiduals_img.png
fits[0].fit_datahttps://www.sasbdb.org/media/fitting_files/SASDV56_fit1.fit
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fits[0].software_versionnull
fits[0].description
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fits[1].models[0].softwareAMBER
fits[1].models[0].pdb_link[]
fits[1].models[0].model_titlenull
fits[1].models[0].type_of_modelatomic
fits[1].models[0].software_versionnull
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fits[1].models[0].model_mw22.3
fits[1].models[0].bead_radiusnull
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fits[1].models[0].commentnull
fits[1].models[0].user9
fits[1].fit_unit1/A
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fits[1].softwareCRYSOL
fits[1].chi_square_value1.272
fits[1].p_value0.0013
fits[1].fit_residual_plotSASDV56_fit2_fitresiduals_img.png
fits[1].fit_datahttps://www.sasbdb.org/media/fitting_files/SASDV56_fit2.fit
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fits[1].software_versionnull
fits[1].description
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from solutions of microtubule-associated protein tau (lysine-rich four-repeat domain 4RD) synthetically linked to ubiquitin at tau amino acid C317 in 100 mM NaCl, pH 6.8 were collected on the EMBL P12 beam line at PETRA III (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.123972 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.00 mg/ml was measured at 20°C. 20 successive 0.050 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.
tags[]
intensity_unit1/cm
experimental_mw20.66
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw25.8
porod_mw_errornull
pddf_i00.0499
pddf_i0_errornull
guinier_i00.0489423
guinier_i0_errornull
pddf_rg3.598
pddf_rg_errornull
guinier_rg3.34
guinier_rg_error0.046
pddf_dmax13.3
pddf_dmax_errornull
porod_volume41.3
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first12
guinier_point_last104
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDV56_datloglog_img.png
symmetrynull
last_modified2025-04-10T13:15:30.028980+02:00
bragg_peak[]
manifest.json:34 field values
Field pathRaw value
codeSASDV56
statussuccess
started_at2026-08-11T15:02:21.089302+00:00
finished_at2026-08-11T15:02:29.455019+00:00
source_last_modified2025-04-10T13:15:30.028980+02:00
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View the complete summary.json source
{
  "code": "SASDV56",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/nm",
  "project": {
    "title": "Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain.",
    "publication": {
      "title": "Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain.",
      "author_list": "Viola G, Trivellato D, Laitaoja M, Jänis J, Felli IC, D'Onofrio M, Mollica L, Giachin G, Assfalg M",
      "journal": "Proc Natl Acad Sci U S A",
      "doi": "10.1073/pnas.2425831122",
      "pmid": "40198698",
      "published_date": "2025 Apr 15"
    },
    "status": "released",
    "submitted_date": "2024-08-13",
    "released_date": "2025-03-21"
  },
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  "pddf_plot": "https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDV56_pofr_img.png",
  "intensities_guinier_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDV56_guinier_img.png",
  "sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDV56.sascif",
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        "name": "Pilatus 6M",
        "resolution": null
      },
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      "city": "DESY; Hamburg",
      "country": "Germany",
      "beamline_name": "EMBL P12",
      "beam_geometry": null,
      "type_of_source": "X-ray synchrotron",
      "point_source": null,
      "line_collimation": null,
      "sample_path_length": null,
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            "short_name": "ESRF",
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            "full_name": "European Synchrotron Radiation Facility",
            "webpage": "http://www.esrf.eu/"
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}
View the complete manifest.json source
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