SASDG95

Phosphorylated resistance to inhibitors of cholinesterase 8 homolog A (Ric-8A, 1-491) and G protein complex

Data type: SASBDB experimental data Status: Published Curve type: SEC-SAS Last updated: 2020-02-27T17:21:05.271305+01:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Phosphorylated resistance to inhibitors of cholinesterase 8 homolog A (Ric-8A, 1-491) and G protein complex

Concentration— – 5.0 Buffer / pH25 mM HEPES, 150 mM NaCl / 8.0
Experimental temperature20.0 Facility / beamlineAdvanced Photon Source (APS), Argonne National Laboratory / BioCAT 18ID
Wavelength0.1033 nmExposure0.5 s × 1500

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Resistance to inhibitors of cholinesterase 8 homolog A
View sequence
MEPRAVADALETGEEDAVTEALRSFNREHSQSFTFDDAQQEDRKRLAKLLVSVLEQGLSPKHRVTWLQTIRILSRDRSCLDSFASRQSLHALACYADIAISEEPIPQPPDMDVLLESLKCLCNLVLSSPTAQMLAAEARLVVRLAERVGLYRKRSYPHEVQFFDLRLLFLLTALRTDVRQQLFQELHGVRLLTDALELTLGVAPKENPLVILPAQETERAMEILKVLFNITYDSVKREVDEEDAALYRYLGTLLRHCVMADAAGDRTEEFHGHTVNLLGNLPLKCLDVLLALELHEGSLEFMGVNMDVINALLAFLEKRLHQTHRLKECVAPVLSVLTECARMHRPARKFLKAQVLPPLRDVRTRPEVGDLLRNKLVRLMTHLDTDVKRVAAEFLFVLCSESVPRFIKYTGYGNAAGLLAARGLMAGGRPEGQYSEDEDTDTEEYREAKASINPVTGRVEEKPPNPMEGMTEEQKEHEAMKLVNMFDKLSR
proteinRattus norvegicusB1H2411–491monomerMolecule count 155.559 kDa
Guanine nucleotide-binding protein G(i) subunit alpha-1
View sequence
REDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
proteinRattus norvegicusP1082424–354monomerMolecule count 137.824 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11229[3]0.00425604108–0.352240131 1/AHas uncertainty columnMissing 040sasbdb/entries/95/sasdg95/source/SASDG95.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)11.5—Å
i0Guinier0.14850.0001028arbitrary
i0P(r)0.149—arbitrary
mwExperimental92.0—kDa
porod_volumePorod120.0—ų
rgGuinier3.480.01Å
rgP(r)3.53—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 name25 mM HEPES, 150 mM NaClBuffer concentration—
pH8.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2019-07-30Storage / measurement temperature4.0 / 20.0
Exposure time0.5Frames1500
Wavelength0.1033Sample-to-detector distance3.67
SourceX-ray synchrotronDetectorPilatus3 X 1M
Facility / beamlineAdvanced Photon Source (APS), Argonne National Laboratory / BioCAT 18ID · Lemont, IL, USA
q range0.043 – 3.522Sample volume / flow rate500.0 / 0.7

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 (4 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:173 field values
Field pathRaw value
codeSASDG95
statusPublished
type_of_curveSEC-SAS
angular_unit1/A
project.titleStructure of the G protein chaperone and guanine nucleotide exchange factor Ric-8A bound to Gαi1
project.publication.titleStructure of the G protein chaperone and guanine nucleotide exchange factor Ric-8A bound to Gαi1
project.publication.author_listMcClelland L, Zhang K, Mou T, Johnston J, Yates-Hansen C, Li S, Thomas C, Doukov T, Triest S, Wohlkonig A, Tall G, Steyaert J, Chiu W, Sprang S
project.publication.journalNature Communications
project.publication.doi10.1038/s41467-020-14943-4
project.publication.pmidnull
project.publication.published_date2020 Feb 26
project.statusreleased
project.submitted_date2019-09-13
project.released_date2020-02-27
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experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus3 X 1M
experiment.instrument.detector.resolution0.172
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_nameResistance to inhibitors of cholinesterase 8 homolog A
experiment.sample.molecule[0].short_nameRic-8A
experiment.sample.molecule[0].sequenceMEPRAVADALETGEEDAVTEALRSFNREHSQSFTFDDAQQEDRKRLAKLLVSVLEQGLSPKHRVTWLQTIRILSRDRSCLDSFASRQSLHALACYADIAISEEPIPQPPDMDVLLESLKCLCNLVLSSPTAQMLAAEARLVVRLAERVGLYRKRSYPHEVQFFDLRLLFLLTALRTDVRQQLFQELHGVRLLTDALELTLGVAPKENPLVILPAQETERAMEILKVLFNITYDSVKREVDEEDAALYRYLGTLLRHCVMADAAGDRTEEFHGHTVNLLGNLPLKCLDVLLALELHEGSLEFMGVNMDVINALLAFLEKRLHQTHRLKECVAPVLSVLTECARMHRPARKFLKAQVLPPLRDVRTRPEVGDLLRNKLVRLMTHLDTDVKRVAAEFLFVLCSESVPRFIKYTGYGNAAGLLAARGLMAGGRPEGQYSEDEDTDTEEYREAKASINPVTGRVEEKPPNPMEGMTEEQKEHEAMKLVNMFDKLSR
experiment.sample.molecule[0].organismRattus norvegicus
experiment.sample.molecule[0].uniprot_codeB1H241
experiment.sample.molecule[0].uniprot_range_first1
experiment.sample.molecule[0].uniprot_range_last491
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMEPRAVADALETGEEDAVTEALRSFNREHSQSFTFDDAQQEDRKRLAKLLVSVLEQGLSP KHRVTWLQTIRILSRDRSCLDSFASRQSLHALACYADIAISEEPIPQPPDMDVLLESLKC LCNLVLSSPTAQMLAAEARLVVRLAERVGLYRKRSYPHEVQFFDLRLLFLLTALRTDVRQ QLFQELHGVRLLTDALELTLGVAPKENPLVILPAQETERAMEILKVLFNITYDSVKREVD EEDAALYRYLGTLLRHCVMADAAGDRTEEFHGHTVNLLGNLPLKCLDVLLALELHEGSLE FMGVNMDVINALLAFLEKRLHQTHRLKECVAPVLSVLTECARMHRPARKFLKAQVLPPLR DVRTRPEVGDLLRNKLVRLMTHLDTDVKRVAAEFLFVLCSESVPRFIKYTGYGNAAGLLA ARGLMAGGRPEGQYSEDEDTDTEEYREAKASINPVTGRVEEKPPNPMEGMTEEQKEHEAM KLVNMFDKLSRHRLIQPMGMSPRGHLTSLQDAMCETMEGQLSSDPDSDPD
experiment.sample.molecule[0].mw55.559
experiment.sample.molecule[0].total_mw55.559
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.molecule[1].long_nameGuanine nucleotide-binding protein G(i) subunit alpha-1
experiment.sample.molecule[1].short_nameGia
experiment.sample.molecule[1].sequenceREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
experiment.sample.molecule[1].organismRattus norvegicus
experiment.sample.molecule[1].uniprot_codeP10824
experiment.sample.molecule[1].uniprot_range_first24
experiment.sample.molecule[1].uniprot_range_last354
experiment.sample.molecule[1].oligomerizationmonomer
experiment.sample.molecule[1].molecular_typeprotein
experiment.sample.molecule[1].uniprot_sequenceMGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAG YSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMT AELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVK TTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEM NRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAA AYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
experiment.sample.molecule[1].mw37.824
experiment.sample.molecule[1].total_mw37.824
experiment.sample.molecule[1].number_molecules1
experiment.sample.molecule[1].complex_stateFalse
experiment.sample.molecule[1].deuterationnull
experiment.sample.molecule[1].molecule_sourcebiological
experiment.sample.molecule[1].molecule_descriptionnull
experiment.sample.buffer.name25 mM HEPES, 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.ph8.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.namePhosphorylated resistance to inhibitors of cholinesterase 8 homolog A (Ric-8A, 1-491) and G protein complex
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].addressMontana, USA
experiment.contributor[0].affiliation[0].full_nameUniversity of Montana
experiment.contributor[0].affiliation[0].webpagehttps://www.umt.edu/
experiment.contributor[0].contributor_nameTung-Chung
experiment.contributor[0].contributor_surnameMou
experiment.contributor[0].orcidhttps://orcid.org/0000-0001-6554-1519
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2019-07-30
experiment.storage_temperature4.0
experiment.cell_temperature20.0
experiment.exposure_time0.5
experiment.number_of_frames1500
experiment.wavelength0.1033
experiment.sample_detector_distance3.67
experiment.concentration_minnull
experiment.concentration_max5.0
experiment.sample_volume500.0
experiment.flow_rate0.7
experiment.s_min0.043
experiment.s_max3.522
experiment.total_exposure_timenull
experiment.seccolumn1
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fits[0].models[0].model_mw79.96
fits[0].models[0].bead_radius3.25
fits[0].models[0].lognull
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fits[0].models[0].commentnull
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pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from solutions of the Ric-8A (1-491) and G protein complex in 25 mM HEPES, 150 mM NaCl, pH 8 were collected on the BioCAT 18ID beam line at the Advanced Photon Source (APS), Argonne National Laboratory (Lemont, IL, USA) using a Pilatus3 X 1M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 500.00 μl sample at 5 mg/ml was injected at a 0.70 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 20°C. 1500 successive 0.500 second frames were collected through the elution profile. The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering from an appropriate solvent-blank was subtracted from the 1D scattering intensities obtained for the sample peak.
tags[]
intensity_unitarbitrary
experimental_mw92.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i00.149
pddf_i0_errornull
guinier_i00.1485
guinier_i0_error0.0001028
pddf_rg3.53
pddf_rg_errornull
guinier_rg3.48
guinier_rg_error0.01
pddf_dmax11.5
pddf_dmax_errornull
porod_volume120.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first9
guinier_point_last114
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDG95_datloglog_img.png
symmetrynull
last_modified2020-02-27T17:21:05.271305+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDG95
statussuccess
started_at2026-08-11T14:42:30.118529+00:00
finished_at2026-08-11T14:42:40.027622+00:00
source_last_modified2020-02-27T17:21:05.271305+01:00
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View the complete summary.json source
{
  "code": "SASDG95",
  "status": "Published",
  "type_of_curve": "SEC-SAS",
  "angular_unit": "1/A",
  "project": {
    "title": "Structure of the G protein chaperone and guanine nucleotide exchange factor Ric-8A bound to Gαi1",
    "publication": {
      "title": "Structure of the G protein chaperone and guanine nucleotide exchange factor Ric-8A bound to Gαi1",
      "author_list": "McClelland L, Zhang K, Mou T, Johnston J, Yates-Hansen C, Li S, Thomas C, Doukov T, Triest S, Wohlkonig A, Tall G, Steyaert J, Chiu W, Sprang S",
      "journal": "Nature Communications",
      "doi": "10.1038/s41467-020-14943-4",
      "pmid": null,
      "published_date": "2020 Feb 26"
    },
    "status": "released",
    "submitted_date": "2019-09-13",
    "released_date": "2020-02-27"
  },
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        "affiliation": [
          {
            "short_name": null,
            "address": "Montana, USA",
            "full_name": "University of Montana",
            "webpage": "https://www.umt.edu/"
          }
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        "contributor_name": "Tung-Chung",
        "contributor_surname": "Mou",
        "orcid": "https://orcid.org/0000-0001-6554-1519"
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View the complete manifest.json source
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