SASDCL7

Truncated monomeric Cytohesin-3 (Grp1; amino acids 63-390)

Data type: SASBDB experimental data Status: Published Curve type: Other Last updated: 2020-08-28T15:28:09.113239+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Truncated monomeric Cytohesin-3 (Grp1; amino acids 63-390)

Concentration0.0 – 2.0 Buffer / pH20 mM Tris, 150 mM NaCl, 2 mM MgCl2, 0.001 mM inositol 1,3,4,5-tetrakisphosphate / 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
Cytohesin-3
View sequence
MGHHHHHHGSTTQRNAQIAMGRKKFNMDPKKGIQFLIENDLLQSSPEDVAQFLYKGEGLNKTVIGDYLGERDDFNIKVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAFASRYCLCNPGVFQSTDTCYVLSFAIIMLNTSLHNHNVRDKPTAERFITMNRGINEGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTYTFFNPDREGWLLKLGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEDPRKPNCFELYNPSHKGQVIKACKTEADGRVVEGNHVVYRISAPSPEEKEEWMKSIKASISRDPFYDMLATRKRRIANKK
proteinMus musculusO0896763–399monomerMolecule count 140.355 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
176[3]0.00825627–0.392501 1/AHas uncertainty columnMissing 00sasbdb/entries/l7/sasdcl7/source/SASDCL7.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)9.30.1Å
i0Guinier1.020.002arbitrary
i0P(r)1.030.002arbitrary
mwExperimental42.8—kDa
mwPorod42.8—kDa
porod_volumePorod64.2—ų
rgGuinier2.760.02Å
rgP(r)2.860.01Å

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

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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, 0.001 mM inositol 1,3,4,5-tetrakisphosphateBuffer concentration—
pH8.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2013-03-21Storage / measurement temperature— / 20.0
Exposure time1.0Frames1
Wavelength0.10332Sample-to-detector distance2.0
SourceX-ray synchrotronDetectorMAR 165 CCD
Facility / beamlineAdvanced Photon Source (APS), Argonne National Laboratory / BioCAT 18ID · Lemont, IL, USA
q range0.083 – 3.925Sample 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:253 field values
Field pathRaw value
codeSASDCL7
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/SASDCL7.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_nameCytohesin-3
experiment.sample.molecule[0].short_nameCyth3
experiment.sample.molecule[0].sequenceMGHHHHHHGSTTQRNAQIAMGRKKFNMDPKKGIQFLIENDLLQSSPEDVAQFLYKGEGLNKTVIGDYLGE RDDFNIKVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAFASRYCLCNPGVFQSTDTCYV LSFAIIMLNTSLHNHNVRDKPTAERFITMNRGINEGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTYTF FNPDREGWLLKLGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEDPRKPNCFELYNP SHKGQVIKACKTEADGRVVEGNHVVYRISAPSPEEKEEWMKSIKASISRDPFYDMLATRKRRIANKK
experiment.sample.molecule[0].organismMus musculus
experiment.sample.molecule[0].uniprot_codeO08967
experiment.sample.molecule[0].uniprot_range_first63
experiment.sample.molecule[0].uniprot_range_last399
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMDEGGGGEGGSVPEDLSLEEREELLDIRRRKKELIDDIERLKYEIAEVMTEIDNLTSVEE SKTTQRNKQIAMGRKKFNMDPKKGIQFLIENDLLQSSPEDVAQFLYKGEGLNKTVIGDYL GERDDFNIKVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAFASRYCLCN PGVFQSTDTCYVLSFAIIMLNTSLHNHNVRDKPTAERFITMNRGINEGGDLPEELLRNLY ESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGRVKTWKRRWFILTDNCLYYFEYTT DKEPRGIIPLENLSIREVEDPRKPNCFELYNPSHKGQVIKACKTEADGRVVEGNHVVYRI SAPSPEEKEEWMKSIKASISRDPFYDMLATRKRRIANKK
experiment.sample.molecule[0].mw40.355
experiment.sample.molecule[0].total_mw40.355
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, 0.001 mM inositol 1,3,4,5-tetrakisphosphate
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 63-390)
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.date2013-03-21
experiment.storage_temperaturenull
experiment.cell_temperature20.0
experiment.exposure_time1.0
experiment.number_of_frames1
experiment.wavelength0.10332
experiment.sample_detector_distance2.0
experiment.concentration_min0.0
experiment.concentration_max2.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.083
experiment.s_max3.925
experiment.total_exposure_timenull
experiment.seccolumnnull
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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 17 mg/ml, and injected in 0.15 ml onto a 24 ml Superdex-200 column equilibrated with 20 mM Tris, pH 8.0, 150 mM NaCl, 2 mM MgCl2, 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 0.5 ml/min. Raw SAXS images were radially averaged on a log scale over the q range 0.00825-0.413 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_mw42.8
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View the complete summary.json source
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