SASDC62

Basic domain of telomeric repeat-binding factor 2 (TRF2)

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2022-03-31T22:26:26.370859+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Basic domain of telomeric repeat-binding factor 2 (TRF2)

Concentration— – 1.2 Buffer / pH50 mM NaPi, 50 mM NaCl / 7.0
Experimental temperature4.0 Facility / beamlineCEITEC / Rigaku BioSAXS-1000
Wavelength1.54 nmExposure3600.0 s × 6

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Basic domain of telomeric repeat-binding factor 2
View sequence
GPPGSMAGGGGSSDGSGRAAGRRASRSSGRARRGRHEPGLGGPAERGAG
proteinHomo sapiensQ1555442–86monomerMolecule count 14.587 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1445[3]0.0109205–0.650319 1/AHas uncertainty columnMissing 06sasbdb/entries/62/sasdc62/source/SASDC62.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)7.06—Å
i0Guinier0.1032870.000861426—
i0P(r)0.1060.001—
mwExperimental4.587—kDa
mwPorod2.3—kDa
porod_volumePorod3.69—ų
rgGuinier1.6570.168Å
rgP(r)1.8190.03Å

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 name50 mM NaPi, 50 mM NaClBuffer concentration—
pH7.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2015-03-05Storage / measurement temperature4.0 / 4.0
Exposure time3600.0Frames6
Wavelength1.54Sample-to-detector distance0.48
SourceX-ray in houseDetectorPilatus 100K
Facility / beamlineCEITEC / Rigaku BioSAXS-1000 · Brno, Czech Republic
q range0.109 – 6.503Sample 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:134 field values
Field pathRaw value
codeSASDC62
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleBasic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it.
project.publication.titleBasic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it.
project.publication.author_listNecasová I, Janoušková E, Klumpler T, Hofr C
project.publication.journalNucleic Acids Res
project.publication.doi10.1093/nar/gkx812
project.publication.pmid28981702
project.publication.published_date2017 Dec 1
project.statusreleased
project.submitted_date2017-01-06
project.released_date2017-09-18
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experiment.instrument.detector.resolution172.0
experiment.instrument.nameCEITEC
experiment.instrument.cityBrno
experiment.instrument.countryCzech Republic
experiment.instrument.beamline_nameRigaku BioSAXS-1000
experiment.instrument.beam_geometry
experiment.instrument.type_of_sourceX-ray in house
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_nameBasic domain of telomeric repeat-binding factor 2
experiment.sample.molecule[0].short_nameTRF2
experiment.sample.molecule[0].sequenceGPPGSMAGGGGSSDGSGRAAGRRASRSSGRARRGRHEPGLGGPAERGAG
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeQ15554
experiment.sample.molecule[0].uniprot_range_first42
experiment.sample.molecule[0].uniprot_range_last86
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMAAGAGTAGPASGPGVVRDPAASQPRKRPGREGGEGARRSDTMAGGGGSSDGSGRAAGRR ASRSSGRARRGRHEPGLGGPAERGAGEARLEEAVNRWVLKFYFHEALRAFRGSRYGDFRQ IRDIMQALLVRPLGKEHTVSRLLRVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEM IKTEFTLTEAVVESSRKLVKEAAVIICIKNKEFEKASKILKKHMSKDPTTQKLRNDLLNI IREKNLAHPVIQNFSYETFQQKMLRFLESHLDDAEPYLLTMAKKALKSESAASSTGKEDK QPAPGPVEKPPREPARQLRNPPTTIGMMTLKAAFKTLSGAQDSEAAFAKLDQKDLVLPTQ ALPASPALKNKRPRKDENESSAPADGEGGSELQPKNKRMTISRLVLEEDSQSTEPSAGLN SSQEAASAPPSKPTVLNQPLPGEKNPKVPKGKWNSSNGVEEKETWVEEDELFQVQAAPDE DSTTNITKKQKWTVEESEWVKAGVQKYGEGNWAAISKNYPFVNRTAVMIKDRWRTMKRLG MN
experiment.sample.molecule[0].mw4.587
experiment.sample.molecule[0].total_mw4.587
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.name50 mM NaPi, 50 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.ph7.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameBasic domain of telomeric repeat-binding factor 2 (TRF2)
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].addressnull
experiment.contributor[0].affiliation[0].full_nameCEITEC - Central European Institute of Technology, Masaryk University
experiment.contributor[0].affiliation[0].webpagehttps://www.ceitec.eu/
experiment.contributor[0].contributor_nameTomas
experiment.contributor[0].contributor_surnameKlumpler
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2015-03-05
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experiment.concentration_minnull
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experiment.s_min0.109
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experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionprimus/qt r8972
i0_calibration_standardnull
descriptionnull
experiment_descriptionSAXS data from solutions of the basic domain of telomeric repeat-binding factor 2 (TRF2) in 50 mM sodium phosphate, 50 mM NaCl, pH 7, were collected using a Rigaku BioSAXS-1000 instrument at CEITEC (Brno, Czech Republic) equipped with a Pilatus 100K detector at a sample-detector distance of 0.5 m (I(s) vs s, where = 4π sin θ/λ; 2θ is the scattering angle and λ = 0.154 nm). Six successive 3600 second frames were collected at a sample temperature of 4°C using a solute concentration of 1.2 mg/ml. The data were normalized to the intensity of the transmitted beam and radially averaged and the corresponding scattering from the solvent-blank was subtracted to produced the scattering profile displayed in this entry.
tags[0]idp
intensity_unitnull
experimental_mw4.587
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw2.3
porod_mw_errornull
pddf_i00.106
pddf_i0_error0.001
guinier_i00.103287
guinier_i0_error0.000861426
pddf_rg1.819
pddf_rg_error0.03
guinier_rg1.657
guinier_rg_error0.168
pddf_dmax7.06
pddf_dmax_errornull
porod_volume3.69
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first6
guinier_point_last48
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDC62_datloglog_img.png
symmetrynull
last_modified2022-03-31T22:26:26.370859+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDC62
statussuccess
started_at2026-08-11T13:31:12.464729+00:00
finished_at2026-08-11T13:31:19.977441+00:00
source_last_modified2022-03-31T22:26:26.370859+02:00
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View the complete summary.json source
{
  "code": "SASDC62",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it.",
    "publication": {
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      "author_list": "Necasová I, Janoušková E, Klumpler T, Hofr C",
      "journal": "Nucleic Acids Res",
      "doi": "10.1093/nar/gkx812",
      "pmid": "28981702",
      "published_date": "2017 Dec 1"
    },
    "status": "released",
    "submitted_date": "2017-01-06",
    "released_date": "2017-09-18"
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View the complete manifest.json source
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