SASDEK8

Farnesylated human Guanylate Binding Protein 1 (farn-hGBP1), batch mode

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2019-12-06T13:07:15.624532+01:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Farnesylated human Guanylate Binding Protein 1 (farn-hGBP1), batch mode

Concentration— – 2.3 Buffer / pH50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl / 7.9
Experimental temperature22.0 Facility / beamlineESRF / BM29
Wavelength0.09919 nmExposure3.0 s × 10

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
farnesylated human Guanylate-binding protein 1
View sequence
MRGSHHHHHHGSASEIHMTGPMCLIENTNGRLMANPEALKILSAITQPMVVVAIVGLYRTGKSYLMNKLAGKKKGFSLGSTVQSHTKGIWMWCVPHPKKPGHILVLLDTEGLGDVEKGDNQNDSWIFALAVLLSSTFVYNSIGTINQQAMDQLYYVTELTHRIRSKSSPDENENEVEDSADFVSFFPDFVWTLRDFSLDLEADGQPLTPDEYLTYSLKLKKGTSQKDETFNLPRLCIRKFFPKKKCFVFDRPVHRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIQVNGPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVQKAIAHYEQQMGQKVQLPTESLQELLDLHRDSEREAIEVFIRSSFKDVDHLFQKELAAQLEKKRDDFCKQNQEASSDRCSGLLQVIFSPLEEEVKAGIYSKPGGYRLFVQKLQDLKKKYYEEPRKGIQAEEILQTYLKSKESMTDAILQTDQTLTEKEKEIEVERVKAESAQASAKMLQEMQRKNEQMMEQKERSYQEHLKQLTEKMENDRVQLLKEQERTLALKLQEQEQLLKEGFQKESRIMKNEIQDLQTKMRRRKACTIS
proteinHomo sapiensP324551–592monomerMolecule count 169.169 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11043[3]0.0032608150000000002–0.4946001 1/AHas uncertainty columnMissing 013sasbdb/entries/k8/sasdek8/source/SASDEK8.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)14.25—Å
i0Guinier13.90.014arbitrary
i0P(r)58.84—arbitrary
mwExperimental63.63—kDa
mwPorod64.0—kDa
porod_volumePorod102.0—ų
rgGuinier3.820.03Å
rgP(r)3.98—Å

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 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 date2016-05-08Storage / measurement temperature22.0 / 22.0
Exposure time3.0Frames10
Wavelength0.09919Sample-to-detector distance2.867
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineESRF / BM29 · Grenoble, France
q range0.033 – 4.946Sample 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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full_entry_zip:source record and ZIP contents (5 items)
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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:170 field values
Field pathRaw value
codeSASDEK8
statusPublished
type_of_curveSingle concentration
angular_unit1/A
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
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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_namefarnesylated human Guanylate-binding protein 1
experiment.sample.molecule[0].short_namefarn-hGBP1
experiment.sample.molecule[0].sequenceMRGSHHHHHHGSASEIHMTGPMCLIENTNGRLMANPEALKILSAITQPMVVVAIVGLYRTGKSYLMNKLAGKKKGFSLGSTVQSHTKGIWMWCVPHPKKPGHILVLLDTEGLGDVEKGDNQNDSWIFALAVLLSSTFVYNSIGTINQQAMDQLYYVTELTHRIRSKSSPDENENEVEDSADFVSFFPDFVWTLRDFSLDLEADGQPLTPDEYLTYSLKLKKGTSQKDETFNLPRLCIRKFFPKKKCFVFDRPVHRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIQVNGPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVQKAIAHYEQQMGQKVQLPTESLQELLDLHRDSEREAIEVFIRSSFKDVDHLFQKELAAQLEKKRDDFCKQNQEASSDRCSGLLQVIFSPLEEEVKAGIYSKPGGYRLFVQKLQDLKKKYYEEPRKGIQAEEILQTYLKSKESMTDAILQTDQTLTEKEKEIEVERVKAESAQASAKMLQEMQRKNEQMMEQKERSYQEHLKQLTEKMENDRVQLLKEQERTLALKLQEQEQLLKEGFQKESRIMKNEIQDLQTKMRRRKACTIS
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].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].mw69.169
experiment.sample.molecule[0].total_mw69.169
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-HCl, 5 mM MgCl2, 150 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.ph7.9
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameFarnesylated human Guanylate Binding Protein 1 (farn-hGBP1), batch mode
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.date2016-05-08
experiment.storage_temperature22.0
experiment.cell_temperature22.0
experiment.exposure_time3.0
experiment.number_of_frames10
experiment.wavelength0.09919
experiment.sample_detector_distance2.867
experiment.concentration_minnull
experiment.concentration_max2.3
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.033
experiment.s_max4.946
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].p_value0.0
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fits[1].softwareOther
fits[1].chi_square_value1.3854
fits[1].p_value0.003834
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fits[1].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from solutions of Farnesylated human Guanylate Binding Protein 1 (farn-hGBP1) in 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, pH 7.9 were collected 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). One solute concentration of 2.30 mg/ml was measured at 22°C. 10 successive 3 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_unitarbitrary
experimental_mw63.63
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw64.0
porod_mw_errornull
pddf_i058.84
pddf_i0_errornull
guinier_i013.9
guinier_i0_error0.014
pddf_rg3.98
pddf_rg_errornull
guinier_rg3.82
guinier_rg_error0.03
pddf_dmax14.25
pddf_dmax_errornull
porod_volume102.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first12
guinier_point_last59
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDEK8_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDEK8
statussuccess
started_at2026-08-11T15:54:58.940921+00:00
finished_at2026-08-11T15:55:07.657853+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDEK8",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "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",
      "journal": "FEBS J",
      "doi": "10.1111/febs.15015",
      "pmid": "31330084",
      "published_date": "2019 Jul 22"
    },
    "status": "released",
    "submitted_date": "2018-11-27",
    "released_date": "2019-07-24"
  },
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      "country": "France",
      "beamline_name": "BM29",
      "beam_geometry": "",
      "type_of_source": "X-ray synchrotron",
      "point_source": null,
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          "uniprot_range_last": 592,
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            "short_name": null,
            "address": "Germany",
            "full_name": "Forschungszentrum Jülich",
            "webpage": "https://www.fz-juelich.de"
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View the complete manifest.json source
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