SASDEG8

Human Guanylate Binding Protein 1 with GppNHp (hGBP1 + GppNHp), dimer from SEC-SAXS

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2020-08-28T15:28:11.819155+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Human Guanylate Binding Protein 1 with GppNHp (hGBP1 + GppNHp), dimer from SEC-SAXS

Concentration— – 55.0 Buffer / pH50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, 0.2 mM GppNHp / 7.9
Experimental temperature20.0 Facility / beamlineESRF / BM29
Wavelength0.09919 nmExposure1.0 s × 3600

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
human Guanylate-binding protein 1
View sequence
>HGBP1-MITHISTAG:A|CHAIN|SEQUENCEMRGSHHHHHHGSASEIHMTGPMCLIENTNGRLMANPEALKILSAITQPMVVVAIVGLYRTGKSYLMNKLAGKKKGFSLGSTVQSHTKGIWMWCVPHPKKPGHILVLLDTEGLGDVEKGDNQNDSWIFALAVLLSSTFVYNSIGTINQQAMDQLYYVTELTHRIRSKSSPDENENEVEDSADFVSFFPDFVWTLRDFSLDLEADGQPLTPDEYLTYSLKLKKGTSQKDETFNLPRLCIRKFFPKKKCFVFDRPVHRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIQVNGPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVQKAIAHYEQQMGQKVQLPTESLQELLDLHRDSEREAIEVFIRSSFKDVDHLFQKELAAQLEKKRDDFCKQNQEASSDRCSGLLQVIFSPLEEEVKAGIYSKPGGYRLFVQKLQDLKKKYYEEPRKGIQAEEILQTYLKSKESMTDAILQTDQTLTEKEKEIEVERVKAESAQASAKMLQEMQRKNEQMMEQKERSYQEHLKQLTEKMENDRVQLLKEQERTLALKLQEQEQLLKEGFQKESRIMKNEIQDLQTKMRRRKACTIS
proteinHomo sapiensP324551–592dimerMolecule count 269.169 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11040[3]0.04680158–4.944452 1/nmHas uncertainty columnMissing 03sasbdb/entries/g8/sasdeg8/source/SASDEG8.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)22.0—nm
i0Guinier155.50.16arbitrary
i0P(r)157.4—arbitrary
mwExperimental159.38—kDa
mwPorod168.49—kDa
porod_volumePorod269.6—nm³
rgGuinier5.450.19nm
rgP(r)5.728—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-HCl, 5 mM MgCl2, 150 mM NaCl, 0.2 mM GppNHpBuffer concentration—
pH7.9Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2017-04-30Storage / measurement temperature20.0 / 20.0
Exposure time1.0Frames3600
Wavelength0.09919Sample-to-detector distance2.867
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineESRF / BM29 · Grenoble, France
q range0.047 – 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:190 field values
Field pathRaw value
codeSASDEG8
statusPublished
type_of_curveSingle concentration
angular_unit1/nm
project.titleFarnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization.
project.publication.titleFarnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization.
project.publication.author_listLorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
project.publication.journalFEBS J
project.publication.doi10.1111/febs.15015
project.publication.pmid31330084
project.publication.published_date2019 Jul 22
project.statusreleased
project.submitted_date2018-11-27
project.released_date2019-07-24
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDEG8.out
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pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDEG8_pofr_img.png
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sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDEG8.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_namehuman Guanylate-binding protein 1
experiment.sample.molecule[0].short_namehGBP1
experiment.sample.molecule[0].sequence>hGBP1-mitHIStag:A|CHAIN|SEQUENCE MRGSHHHHHHGSASEIHMTGPMCLIENTNGRLMANPEALKILSAITQPMVVVAIVGLYRTGKSYLMNKLAGKKKGFSLGSTVQSHTKGIWMWCVPHPKKPGHILVLLDTEGLGDVEKGDNQNDSWIFALAVLLSSTFVYNSIGTINQQAMDQLYYVTELTHRIRSKSSPDENENEVEDSADFVSFFPDFVWTLRDFSLDLEADGQPLTPDEYLTYSLKLKKGTSQKDETFNLPRLCIRKFFPKKKCFVFDRPVHRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIQVNGPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVQKAIAHYEQQMGQKVQLPTESLQELLDLHRDSEREAIEVFIRSSFKDVDHLFQKELAAQLEKKRDDFCKQNQEASSDRCSGLLQVIFSPLEEEVKAGIYSKPGGYRLFVQKLQDLKKKYYEEPRKGIQAEEILQTYLKSKESMTDAILQTDQTLTEKEKEIEVERVKAESAQASAKMLQEMQRKNEQMMEQKERSYQEHLKQLTEKMENDRVQLLKEQERTLALKLQEQEQLLKEGFQKESRIMKNEIQDLQTKMRRRKACTIS
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeP32455
experiment.sample.molecule[0].uniprot_range_first1
experiment.sample.molecule[0].uniprot_range_last592
experiment.sample.molecule[0].oligomerizationdimer
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].mw69.169
experiment.sample.molecule[0].total_mw138.338
experiment.sample.molecule[0].number_molecules2
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-HCl, 5 mM MgCl2, 150 mM NaCl, 0.2 mM GppNHp
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.9
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameHuman Guanylate Binding Protein 1 with GppNHp (hGBP1 + GppNHp), dimer from SEC-SAXS
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_nameCharlotte
experiment.contributor[0].contributor_surnameLorenz
experiment.contributor[0].orcidhttps://orcid.org/0000-0003-3614-341X
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2017-04-30
experiment.storage_temperature20.0
experiment.cell_temperature20.0
experiment.exposure_time1.0
experiment.number_of_frames3600
experiment.wavelength0.09919
experiment.sample_detector_distance2.867
experiment.concentration_minnull
experiment.concentration_max55.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.047
experiment.s_max4.944
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].softwareCRYSOL
fits[0].chi_square_value1058.2468
fits[0].p_value0.0
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fits[0].descriptionnull
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fits[1].softwareEOM/GAJOE
fits[1].chi_square_value1.493
fits[1].p_value4.5e-05
fits[1].fit_residual_plotSASDEG8_fit2_fitresiduals_img.png
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fits[1].descriptionnull
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fits[2].softwareSASREF
fits[2].chi_square_value6.45
fits[2].p_value0.0
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fits[2].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from solutions of Human Guanylate Binding Protein 1 with guanylyl imidodiphosphate (hGBP1 + GppNHp) in 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, 0.2 mM GppNHp pH 7.9 were collected using size-exclusion chromatography SAXS (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 = 0.09919 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). SEC-SAXS was performed at 20°C using the following parameters: Column: UNKNOWN; Flow rate: UNKNOWN mL/min; Total acquisition time: 3600 s; Sample injection concentration: 55 mg/mL; Injection volume: UNKNOWN μL. The data obtained through the sample elution peak (collected as successive 1 s frames) were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the individual subtracted data sets were scaled and averaged to generate the scattering profile displayed in this entry.
tags[]
intensity_unitarbitrary
experimental_mw159.38
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw168.49
porod_mw_errornull
pddf_i0157.4
pddf_i0_errornull
guinier_i0155.5
guinier_i0_error0.16
pddf_rg5.728
pddf_rg_errornull
guinier_rg5.45
guinier_rg_error0.19
pddf_dmax22.0
pddf_dmax_errornull
porod_volume269.6
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first18
guinier_point_last32
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDEG8_datloglog_img.png
symmetrynull
last_modified2020-08-28T15:28:11.819155+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDEG8
statussuccess
started_at2026-08-11T15:52:54.842805+00:00
finished_at2026-08-11T15:53:04.331314+00:00
source_last_modified2020-08-28T15:28:11.819155+02:00
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View the complete summary.json source
{
  "code": "SASDEG8",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/nm",
  "project": {
    "title": "Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization.",
    "publication": {
      "title": "Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization.",
      "author_list": "Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM",
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View the complete manifest.json source
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