SASDCN7

Truncated monomeric Cytohesin-3 (Grp1; amino acids 63-399) E161A 6GS Arf6 Q67L His6 fusion protein

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

Sample 1 · Truncated monomeric Cytohesin-3 (Grp1; amino acids 63-399) E161A 6GS Arf6 Q67L His6 fusion protein

Concentration0.0 – 2.4 Buffer / pH20 mM Tris, 150 mM NaCl, 2 mM MgCl2, 0.1% 2-mercaptoethanol, 5% glycerol, 0.001 mM insitol 1,3,4,5-tetrakis phosphate / 8.0
Experimental temperature20.0 Facility / beamlineAdvanced Photon Source (APS), Argonne National Laboratory / BioCAT 18ID
Wavelength0.10332 nmExposure1.0 s × 1

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Grp1 63-399 E161A 6GS Arf6 Q67L His fusion protein
View sequence
MGHHHHHHGSTTQRNAQIAMGRKKFNMDPKKGIQFLIENDLLQSSPEDVAQFLYKGEGLNKTVIGDYLGERDDFNIKVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAFASRYCLCNPGVFQSTDTCYVLSFAIIMLNTSLHNHNVRDKPTAERFITMNRGINEGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEDPRKPNCFELYNPSHKGQVIKACKTEADGRVVEGNHVVYRISAPSPEEKEEWMKSIKASISRDPFYDMLATRKRRIANKKGSGSGSGSGSGSGKVLSKIFGNKEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFNVWDVGGLDKIRPLWRHYYTGTQGLIFVVDCADRDRIDEARQELHRIINDREMRDAIILIFANKQDLPDAMKPHEIQEKLGLTRIRDRNWYVQPSCATSGDGLYEGLTWLTSNYNHHHHHH
proteinMus musculus——–—monomerMolecule count 161.834 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
176[3]0.00688375–0.316224 1/AHas uncertainty columnMissing 00sasbdb/entries/n7/sasdcn7/source/SASDCN7.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)13.60.1Å
i0Guinier1.010.001arbitrary
i0P(r)1.010.001arbitrary
mwExperimental67.0—kDa
mwPorod67.0—kDa
porod_volumePorod100.5—ų
rgGuinier3.370.008Å
rgP(r)3.430.01Å

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 name20 mM Tris, 150 mM NaCl, 2 mM MgCl2, 0.1% 2-mercaptoethanol, 5% glycerol, 0.001 mM insitol 1,3,4,5-tetrakis phosphateBuffer concentration—
pH8.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2013-11-15Storage / measurement temperature— / 20.0
Exposure time1.0Frames1
Wavelength0.10332Sample-to-detector distance2.5
SourceX-ray synchrotronDetectorMAR 165 CCD
Facility / beamlineAdvanced Photon Source (APS), Argonne National Laboratory / BioCAT 18ID · Lemont, IL, USA
q range0.069 – 3.162Sample 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 (2 items)
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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
codeSASDCN7
statusPublished
type_of_curveOther
angular_unit1/A
project.titleStructural Dynamics Control Allosteric Activation of Cytohesin Family Arf GTPase Exchange Factors.
project.publication.titleStructural Dynamics Control Allosteric Activation of Cytohesin Family Arf GTPase Exchange Factors.
project.publication.author_listMalaby AW, Das S, Chakravarthy S, Irving TC, Bilsel O, Lambright DG
project.publication.journalStructure
project.publication.doi10.1016/j.str.2017.11.019
project.publication.pmid29276036
project.publication.published_date2018 Jan 2
project.statusreleased
project.submitted_date2017-09-22
project.released_date2018-01-02
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDCN7.out
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experiment.instrument.detector.typenull
experiment.instrument.detector.nameMAR 165 CCD
experiment.instrument.detector.resolutionnull
experiment.instrument.nameAdvanced Photon Source (APS), Argonne National Laboratory
experiment.instrument.cityLemont, IL
experiment.instrument.countryUSA
experiment.instrument.beamline_nameBioCAT 18ID
experiment.instrument.beam_geometrynull
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_nameGrp1 63-399 E161A 6GS Arf6 Q67L His fusion protein
experiment.sample.molecule[0].short_namenull
experiment.sample.molecule[0].sequenceMGHHHHHHGSTTQRNAQIAMGRKKFNMDPKKGIQFLIENDLLQSSPEDVAQFLYKGEGLNKTVIGDYLGER DDFNIKVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAFASRYCLCNPGVFQSTDTCYVL SFAIIMLNTSLHNHNVRDKPTAERFITMNRGINEGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEDPRKPNCFELYNPSH KGQVIKACKTEADGRVVEGNHVVYRISAPSPEEKEEWMKSIKASISRDPFYDMLATRKRRIANKKGSGSGSGSGSGSGKVLSKIFGNKEMRILM LGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFNVWDVGGLDKIRPLWRHYYTGTQGLIFVV DCADRDRIDEARQELHRIINDREMRDAIILIFANKQDLPDAMKPHEIQEKLGLTRIRDRNWYVQPSCATS GDGLYEGLTWLTSNYNHHHHHH
experiment.sample.molecule[0].organismMus musculus
experiment.sample.molecule[0].uniprot_codenull
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_sequencenull
experiment.sample.molecule[0].mw61.834
experiment.sample.molecule[0].total_mw61.834
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.name20 mM Tris, 150 mM NaCl, 2 mM MgCl2, 0.1% 2-mercaptoethanol, 5% glycerol, 0.001 mM insitol 1,3,4,5-tetrakis phosphate
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph8.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameTruncated monomeric Cytohesin-3 (Grp1; amino acids 63-399) E161A 6GS Arf6 Q67L His6 fusion protein
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_nameUMASS
experiment.contributor[0].affiliation[0].addressWorcester, MA, USA
experiment.contributor[0].affiliation[0].full_nameUMASS Medical School
experiment.contributor[0].affiliation[0].webpagehttps://www.umassmed.edu/
experiment.contributor[0].contributor_nameDavid
experiment.contributor[0].contributor_surnameLambright
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2013-11-15
experiment.storage_temperaturenull
experiment.cell_temperature20.0
experiment.exposure_time1.0
experiment.number_of_frames1
experiment.wavelength0.10332
experiment.sample_detector_distance2.5
experiment.concentration_min0.0
experiment.concentration_max2.4
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.069
experiment.s_max3.162
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionThis experimental profile was derived from SEC-SAXS data collected at the BioCAT Sector 18-ID beamline at the Argonne National Laboratory Advanced Photon Source using a MAR 165 CCD detector. The protein was equilibrated with a 1.2 molar excess of inositol 1,3,4,5-tetrakis phosphate (IP4), concentrated to 10 mg/ml, and injected in 0.1 ml onto a 3 ml Superdex-200 Increase column equilibrated with 20 mM Tris, pH 8.0, 150 mM NaCl, 2 mM MgCl2, 0.1% 2-mercaptoethanol, 5% glycerol, and 0.001 ml IP4. SAXS data sets were acquired with 1 s exposures at 5 s intervals during elution at a flow rate of 0.25 ml/min. Raw SAXS images were radially averaged on a log scale over the q range 0.00621-0.333 Å-1 and normalized by the incident beam intensity. The protein scattering profile was reconstructed by singular value decomposition and linear combination (SVD-LC) as described in Malaby et al. (2015) Methods for analysis of size-exclusion chromatography-small angle X-ray scattering and reconstruction of protein scattering. J Appl Crystallogr 48: 1102-1113.
tags[]
intensity_unitarbitrary
experimental_mw67.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw67.0
porod_mw_errornull
pddf_i01.01
pddf_i0_error0.001
guinier_i01.01
guinier_i0_error0.001
pddf_rg3.43
pddf_rg_error0.01
guinier_rg3.37
guinier_rg_error0.008
pddf_dmax13.6
pddf_dmax_error0.1
porod_volume100.5
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first1
guinier_point_last29
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDCN7_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDCN7
statussuccess
started_at2026-08-11T15:34:29.236904+00:00
finished_at2026-08-11T15:34:35.990692+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDCN7",
  "status": "Published",
  "type_of_curve": "Other",
  "angular_unit": "1/A",
  "project": {
    "title": "Structural Dynamics Control Allosteric Activation of Cytohesin Family Arf GTPase Exchange Factors.",
    "publication": {
      "title": "Structural Dynamics Control Allosteric Activation of Cytohesin Family Arf GTPase Exchange Factors.",
      "author_list": "Malaby AW, Das S, Chakravarthy S, Irving TC, Bilsel O, Lambright DG",
      "journal": "Structure",
      "doi": "10.1016/j.str.2017.11.019",
      "pmid": "29276036",
      "published_date": "2018 Jan 2"
    },
    "status": "released",
    "submitted_date": "2017-09-22",
    "released_date": "2018-01-02"
  },
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      },
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          "short_name": null,
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          "uniprot_code": null,
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          "oligomerization": "monomer",
          "molecular_type": "protein",
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        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 8.0,
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      },
      "purity_method": null,
      "name": "Truncated monomeric Cytohesin-3 (Grp1; amino acids 63-399) E161A 6GS Arf6 Q67L His6 fusion protein",
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        "orcid": null
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  "pddf_software": "ATSAS GNOM",
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  "description": null,
  "experiment_description": "This experimental profile was derived from SEC-SAXS data collected at the BioCAT Sector 18-ID beamline at the Argonne National Laboratory Advanced Photon Source using a MAR 165 CCD detector.  The protein was equilibrated with a 1.2 molar excess of inositol 1,3,4,5-tetrakis phosphate (IP4), concentrated to 10 mg/ml, and injected in 0.1 ml onto a 3 ml Superdex-200 Increase column equilibrated with 20 mM Tris, pH 8.0, 150 mM NaCl, 2 mM MgCl2, 0.1% 2-mercaptoethanol, 5% glycerol, and 0.001 ml IP4.  SAXS data sets were acquired with 1 s exposures at 5 s intervals during elution at a flow rate of 0.25 ml/min.  Raw SAXS images were radially averaged on a log scale over the q range 0.00621-0.333 Å-1 and normalized by the incident beam intensity.  The protein scattering profile was reconstructed by singular value decomposition and linear combination (SVD-LC) as described in Malaby et al. (2015) Methods for analysis of size-exclusion chromatography-small angle X-ray scattering and reconstruction of protein scattering. J Appl Crystallogr 48: 1102-1113.",
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  "pddf_point_first": null,
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  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDCN7_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2019-12-06T13:07:15.624532+01:00",
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}
View the complete manifest.json source
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