SASDDD6

Human Guanylate-binding protein (hGBP1)

Data type: SASBDB experimental data Status: Published Curve type: SEC-SAS Last updated: 2023-06-19T11:14:52.084807+02:00

Column type: Size exclusion chromatography (Superdex 200 10/300 GL, GE Healthcare) flow rate: 0.5 ml/min.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Human Guanylate-binding protein (hGBP1)

Concentration— – 16.1 Buffer / pH50 mM TRIS, 5 mM MgCl2, 150 mM NaCl / 7.9
Experimental temperature20.0 Facility / beamlineESRF / BM29
Wavelength0.099 nmExposure1.0 s × 114

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Guanylate-binding protein 1
View sequence
>SP|P32455|1-589MASEIHMTGPMCLIENTNGRLMANPEALKILSAITQPMVVVAIVGLYRTGKSYLMNKLAGKKKGFSLGSTVQSHTKGIWMWCVPHPKKPGHILVLLDTEGLGDVEKGDNQNDSWIFALAVLLSSTFVYNSIGTINQQAMDQLYYVTELTHRIRSKSSPDENENEVEDSADFVSFFPDFVWTLRDFSLDLEADGQPLTPDEYLTYSLKLKKGTSQKDETFNLPRLCIRKFFPKKKCFVFDRPVHRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIQVNGPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVQKAIAHYEQQMGQKVQLPTETLQELLDLHRDSEREAIEVFIRSSFKDVDHLFQKELAAQLEKKRDDFCKQNQEASSDRCSALLQVIFSPLEEEVKAGIYSKPGGYRLFVQKLQDLKKKYYEEPRKGIQAEEILQTYLKSKESMTDAILQTDQTLTEKEKEIEVERVKAESAQASAKMLQEMQRKNEQMMEQKERSYQEHLKQLTEKMENDRVQLLKEQERTLALKLQEQEQLLKEGFQKESRIMKNEIQDLQTKMRRRKAC
proteinHomo sapiensP32455—–—monomerMolecule count 167.629 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11043[3]0.0606383–4.944452 1/nmHas uncertainty columnMissing 01sasbdb/entries/d6/sasddd6/source/SASDDD6.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)14.4—nm
i0Guinier65.90.06arbitrary
i0P(r)66.1—arbitrary
mwExperimental65.3—kDa
mwPorod66.1—kDa
porod_volumePorod104.9—nm³
rgGuinier3.890.06nm
rgP(r)4.018—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 name50 mM TRIS, 5 mM MgCl2, 150 mM NaClBuffer concentration—
pH7.9Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2018-04-30Storage / measurement temperature20.0 / 20.0
Exposure time1.0Frames114
Wavelength0.099Sample-to-detector distance2.876
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineESRF / BM29 · Grenoble, France
q range0.061 – 4.944Sample 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:169 field values
Field pathRaw value
codeSASDDD6
statusPublished
type_of_curveSEC-SAS
angular_unit1/nm
project.titleIntegrative dynamic structural biology unveils conformers essential for the oligomerization of a large GTPase.
project.publication.titleIntegrative dynamic structural biology unveils conformers essential for the oligomerization of a large GTPase.
project.publication.author_listPeulen TO, Hengstenberg CS, Biehl R, Dimura M, Lorenz C, Valeri A, Folz J, Hanke CA, Ince S, Vöpel T, Farago B, Gohlke H, Klare JP, Stadler AM, Seidel CAM, Herrmann C
project.publication.journalElife
project.publication.doi10.7554/eLife.79565
project.publication.pmid37314846
project.publication.published_date2023 Jun 14
project.statusreleased
project.submitted_date2018-05-08
project.released_date2019-12-02
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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_nameGuanylate-binding protein 1
experiment.sample.molecule[0].short_namenull
experiment.sample.molecule[0].sequence>sp|P32455|1-589 MASEIHMTGPMCLIENTNGRLMANPEALKILSAITQPMVVVAIVGLYRTGKSYLMNKLAG KKKGFSLGSTVQSHTKGIWMWCVPHPKKPGHILVLLDTEGLGDVEKGDNQNDSWIFALAV LLSSTFVYNSIGTINQQAMDQLYYVTELTHRIRSKSSPDENENEVEDSADFVSFFPDFVW TLRDFSLDLEADGQPLTPDEYLTYSLKLKKGTSQKDETFNLPRLCIRKFFPKKKCFVFDR PVHRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIQVNGPRLESLVLTY VNAISSGDLPCMENAVLALAQIENSAAVQKAIAHYEQQMGQKVQLPTETLQELLDLHRDS EREAIEVFIRSSFKDVDHLFQKELAAQLEKKRDDFCKQNQEASSDRCSALLQVIFSPLEE EVKAGIYSKPGGYRLFVQKLQDLKKKYYEEPRKGIQAEEILQTYLKSKESMTDAILQTDQ TLTEKEKEIEVERVKAESAQASAKMLQEMQRKNEQMMEQKERSYQEHLKQLTEKMENDRV QLLKEQERTLALKLQEQEQLLKEGFQKESRIMKNEIQDLQTKMRRRKAC
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeP32455
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_sequenceMASEIHMTGPMCLIENTNGRLMANPEALKILSAITQPMVVVAIVGLYRTGKSYLMNKLAG KKKGFSLGSTVQSHTKGIWMWCVPHPKKPGHILVLLDTEGLGDVEKGDNQNDSWIFALAV LLSSTFVYNSIGTINQQAMDQLYYVTELTHRIRSKSSPDENENEVEDSADFVSFFPDFVW TLRDFSLDLEADGQPLTPDEYLTYSLKLKKGTSQKDETFNLPRLCIRKFFPKKKCFVFDR PVHRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIQVNGPRLESLVLTY VNAISSGDLPCMENAVLALAQIENSAAVQKAIAHYEQQMGQKVQLPTETLQELLDLHRDS EREAIEVFIRSSFKDVDHLFQKELAAQLEKKRDDFCKQNQEASSDRCSALLQVIFSPLEE EVKAGIYSKPGGYRLFVQKLQDLKKKYYEEPRKGIQAEEILQTYLKSKESMTDAILQTDQ TLTEKEKEIEVERVKAESAQASAKMLQEMQRKNEQMMEQKERSYQEHLKQLTEKMENDRV QLLKEQERTLALKLQEQEQLLKEGFQKESRIMKNEIQDLQTKMRRRKACTIS
experiment.sample.molecule[0].mw67.629
experiment.sample.molecule[0].total_mw67.629
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 TRIS, 5 mM MgCl2, 150 mM NaCl
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
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experiment.sample.buffer.pkanull
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experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameHuman Guanylate-binding protein (hGBP1)
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].addressGermany
experiment.contributor[0].affiliation[0].full_nameForschungszentrum Jülich
experiment.contributor[0].affiliation[0].webpagehttps://www.fz-juelich.de
experiment.contributor[0].contributor_nameAndreas
experiment.contributor[0].contributor_surnameStadler
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2018-04-30
experiment.storage_temperature20.0
experiment.cell_temperature20.0
experiment.exposure_time1.0
experiment.number_of_frames114
experiment.wavelength0.099
experiment.sample_detector_distance2.876
experiment.concentration_minnull
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experiment.sample_volumenull
experiment.flow_ratenull
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experiment.total_exposure_timenull
experiment.seccolumnnull
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pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionColumn type: Size exclusion chromatography (Superdex 200 10/300 GL, GE Healthcare) flow rate: 0.5 ml/min.
experiment_descriptionSynchrotron SAXS data from solutions of Human Guanylate-binding protein (hGBP1) in 50 mM TRIS, 5 mM MgCl2, 150 mM NaCl, pH 7.9 were collected using SEC-SAXS 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 = 0.099 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). The SEC-column load concentration was 16.10 mg/ml (100 µl injection volume). 114 successive 1 second frames were collected through the elution peak, measured at 20°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of an appropriate solvent-blank was subtracted.
tags[]
intensity_unitarbitrary
experimental_mw65.3
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw66.1
porod_mw_errornull
pddf_i066.1
pddf_i0_errornull
guinier_i065.9
guinier_i0_error0.06
pddf_rg4.018
pddf_rg_errornull
guinier_rg3.89
guinier_rg_error0.06
pddf_dmax14.4
pddf_dmax_errornull
porod_volume104.9
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first31
guinier_point_last52
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDDD6_datloglog_img.png
symmetrynull
last_modified2023-06-19T11:14:52.084807+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDDD6
statussuccess
started_at2026-08-11T15:06:47.440307+00:00
finished_at2026-08-11T15:06:56.947654+00:00
source_last_modified2023-06-19T11:14:52.084807+02:00
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View the complete summary.json source
{
  "code": "SASDDD6",
  "status": "Published",
  "type_of_curve": "SEC-SAS",
  "angular_unit": "1/nm",
  "project": {
    "title": "Integrative dynamic structural biology unveils conformers essential for the oligomerization of a large GTPase.",
    "publication": {
      "title": "Integrative dynamic structural biology unveils conformers essential for the oligomerization of a large GTPase.",
      "author_list": "Peulen TO, Hengstenberg CS, Biehl R, Dimura M, Lorenz C, Valeri A, Folz J, Hanke CA, Ince S, Vöpel T, Farago B, Gohlke H, Klare JP, Stadler AM, Seidel CAM, Herrmann C",
      "journal": "Elife",
      "doi": "10.7554/eLife.79565",
      "pmid": "37314846",
      "published_date": "2023 Jun 14"
    },
    "status": "released",
    "submitted_date": "2018-05-08",
    "released_date": "2019-12-02"
  },
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      "country": "France",
      "beamline_name": "BM29",
      "beam_geometry": "",
      "type_of_source": "X-ray synchrotron",
      "point_source": null,
      "line_collimation": null,
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    "sample": {
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          "uniprot_code": "P32455",
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        "affiliation": [
          {
            "short_name": null,
            "address": "Germany",
            "full_name": "Forschungszentrum Jülich",
            "webpage": "https://www.fz-juelich.de"
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    "s_max": 4.944,
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View the complete manifest.json source
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