SASDCD3

Nucleolysin TIA-1 isoform p40 (LPQTG containing construct for sortase mediated protein ligation)

Data type: SASBDB experimental data Status: Published Curve type: Merged Last updated: 2023-12-14T13:41:02.534142+01:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Nucleolysin TIA-1 isoform p40 (LPQTG containing construct for sortase mediated protein ligation)

Concentration1.0 – 5.0 Buffer / pH10 mM Potassium Phosphate 50 mM NaCl 10 mM DTT / 6.0
Experimental temperature20.0 Facility / beamlineSFB 1035, Technische Universität München / Rigaku BioSAXS-1000
Wavelength0.1542 nmExposure900.0 s × 8

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Nucleolysin TIA-1 isoform p40
View sequence
MEDEMPKTLYVGNLSRDVTEALILQLFSQIGPCKNCKMIMDTAGNDPYCFVEFHEHRHAAAALAAMNGRKIMGKEVKVNWATTPSSQKLPQTGNHFHVFVGDLSPEITTEDIKAAFAPFGRISDARVVKDMATGKSKGYGFVSFFNKWDAENAIQQMGGQWLGGRQIRTNWATRKPPAPKSTYESNTKQLSYDEVVNQSSPSNCTVYCGGVTSGLTEQLMRQTFSPFGQIMEIRVFPDKGYSFVRFNSHESAAHAIVSVNGTTIEGHVVKCYWGK
proteinHomo sapiensP31483—–—monomerMolecule count 130.522 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1469[3]0.016574–0.685254 1/AHas uncertainty columnMissing 00sasbdb/entries/d3/sasdcd3/source/SASDCD3.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)10.3—Å
i0Guinier0.02288——
i0P(r)0.0230.0002—
mwExperimental29.9—kDa
mwGuinier I(0)29.9—kDa
mwPorod30.7—kDa
porod_volumePorod38.0—ų
rgGuinier2.710.03Å
rgP(r)2.780.04Å

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 name10 mM Potassium Phosphate 50 mM NaCl 10 mM DTTBuffer concentration—
pH6.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2015-12-01Storage / measurement temperature— / 20.0
Exposure time900.0Frames8
Wavelength0.1542Sample-to-detector distance—
SourceX-ray in houseDetectorPilatus 100K
Facility / beamlineSFB 1035, Technische Universität München / Rigaku BioSAXS-1000 · Garching, Germany
q range0.166 – 6.853Sample 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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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:134 field values
Field pathRaw value
codeSASDCD3
statusPublished
type_of_curveMerged
angular_unit1/A
project.titleSegmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins.
project.publication.titleSegmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins.
project.publication.author_listSonntag M, Jagtap PKA, Simon B, Appavou MS, Geerlof A, Stehle R, Gabel F, Hennig J, Sattler M
project.publication.journalAngew Chem Int Ed Engl
project.publication.doi10.1002/anie.201702904
project.publication.pmid28636238
project.publication.published_date2017 Aug 1
project.statusreleased
project.submitted_date2017-05-04
project.released_date2017-07-24
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experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus 100K
experiment.instrument.detector.resolution172.0
experiment.instrument.nameSFB 1035, Technische Universität München
experiment.instrument.cityGarching
experiment.instrument.countryGermany
experiment.instrument.beamline_nameRigaku BioSAXS-1000
experiment.instrument.beam_geometrypoint
experiment.instrument.type_of_sourceX-ray in house
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_energy8.0405
experiment.instrument.beam_profile_ahnull
experiment.instrument.beam_profile_alnull
experiment.sample.molecule[0].long_nameNucleolysin TIA-1 isoform p40
experiment.sample.molecule[0].short_nameTIA-1 C-LPQTG
experiment.sample.molecule[0].sequenceMEDEMPKTLYVGNLSRDVTEALILQLFSQIGPCKNCKMIMDTAGNDPYCF VEFHEHRHAAAALAAMNGRKIMGKEVKVNWATTPSSQKLPQTGNHFHVFV GDLSPEITTEDIKAAFAPFGRISDARVVKDMATGKSKGYGFVSFFNKWDA ENAIQQMGGQWLGGRQIRTNWATRKPPAPKSTYESNTKQLSYDEVVNQSS PSNCTVYCGGVTSGLTEQLMRQTFSPFGQIMEIRVFPDKGYSFVRFNSHE SAAHAIVSVNGTTIEGHVVKCYWGK
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeP31483
experiment.sample.molecule[0].uniprot_range_firstnull
experiment.sample.molecule[0].uniprot_range_lastnull
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMEDEMPKTLYVGNLSRDVTEALILQLFSQIGPCKNCKMIMDTAGNDPYCFVEFHEHRHAA AALAAMNGRKIMGKEVKVNWATTPSSQKKDTSSSTVVSTQRSQDHFHVFVGDLSPEITTE DIKAAFAPFGRISDARVVKDMATGKSKGYGFVSFFNKWDAENAIQQMGGQWLGGRQIRTN WATRKPPAPKSTYESNTKQLSYDEVVNQSSPSNCTVYCGGVTSGLTEQLMRQTFSPFGQI MEIRVFPDKGYSFVRFNSHESAAHAIVSVNGTTIEGHVVKCYWGKETLDMINPVQQQNQI GYPQPYGQWGQWYGNAQQIGQYMPNGWQVPAYGMYGQAWNQQGFNQTQSSAPWMGPNYGV QPPQGQNGSMLPNQPSGYRVAGYETQ
experiment.sample.molecule[0].mw30.522
experiment.sample.molecule[0].total_mw30.522
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.name10 mM Potassium Phosphate 50 mM NaCl 10 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.ph6.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameNucleolysin TIA-1 isoform p40 (LPQTG containing construct for sortase mediated protein ligation)
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].addressMunich, Germany
experiment.contributor[0].affiliation[0].full_nameTechnical University Munich
experiment.contributor[0].affiliation[0].webpagehttps://www.tum.de
experiment.contributor[0].contributor_nameMiriam
experiment.contributor[0].contributor_surnameSonntag
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2015-12-01
experiment.storage_temperaturenull
experiment.cell_temperature20.0
experiment.exposure_time900.0
experiment.number_of_frames8
experiment.wavelength0.1542
experiment.sample_detector_distancenull
experiment.concentration_min1.0
experiment.concentration_max5.0
experiment.sample_volumenull
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experiment.s_min0.166
experiment.s_max6.853
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionnull
i0_calibration_standardnull
descriptionnull
experiment_descriptionSAXS data from solutions of Nucleolysin TIA-1 isoform p40 (LPQTG containing construct for sortase mediated protein ligation) in 10 mM potassium phosphate, 50 mM NaCl, 10 mM DTT, pH 6 were collected using a Rigaku BioSAXS-1000 instrument (Munich, Germany) equipped with a Pilatus 100K detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). X-ray wavelength = unknown Sample-to-detector distance = unknown Sample concentration(s) = unknown
tags[]
intensity_unitnull
experimental_mw29.9
experimental_mw_errornull
guinier_i0_mw29.9
guinier_i0_mw_errornull
porod_mw30.7
porod_mw_errornull
pddf_i00.023
pddf_i0_error0.0002
guinier_i00.02288
guinier_i0_errornull
pddf_rg2.78
pddf_rg_error0.04
guinier_rg2.71
guinier_rg_error0.03
pddf_dmax10.3
pddf_dmax_errornull
porod_volume38.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first5
guinier_point_last22
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDCD3_datloglog_img.png
symmetrynull
last_modified2023-12-14T13:41:02.534142+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDCD3
statussuccess
started_at2026-08-11T13:57:49.912587+00:00
finished_at2026-08-11T13:57:57.781246+00:00
source_last_modified2023-12-14T13:41:02.534142+01:00
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View the complete summary.json source
{
  "code": "SASDCD3",
  "status": "Published",
  "type_of_curve": "Merged",
  "angular_unit": "1/A",
  "project": {
    "title": "Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins.",
    "publication": {
      "title": "Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins.",
      "author_list": "Sonntag M, Jagtap PKA, Simon B, Appavou MS, Geerlof A, Stehle R, Gabel F, Hennig J, Sattler M",
      "journal": "Angew Chem Int Ed Engl",
      "doi": "10.1002/anie.201702904",
      "pmid": "28636238",
      "published_date": "2017 Aug 1"
    },
    "status": "released",
    "submitted_date": "2017-05-04",
    "released_date": "2017-07-24"
  },
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View the complete manifest.json source
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