SASDXV4

EGFR kinase domain duplication mutant (KDD) at 2.6 mg/ml

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2025-11-02T21:11:43.418457+01:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · EGFR kinase domain duplication mutant (KDD) at 2.6 mg/ml

Concentration— – 2.6 Buffer / pH20 mM HEPES, 250 mM NaCl, 250 mM KCl / 8.0
Experimental temperature4.0 Facility / beamlineYale University / Rigaku MicroMax-007HF
Wavelength0.1542 nmExposure7200.0 s × 3

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Receptor protein-tyrosine kinase (duplication mutant)
View sequence
HHHHHHSSGVDLGTENLYFQSMGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLLVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQG
proteinHomo sapiensQ504U8651–993monomerMolecule count 179.594 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1601[3]0.0069953898–0.500787611 1/AHas uncertainty columnMissing 097sasbdb/entries/v4/sasdxv4/source/SASDXV4.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)16.4—Å
i0Guinier0.278134—arbitrary
i0P(r)0.2736—arbitrary
mwExperimental86.0—kDa
mwGuinier I(0)86.0—kDa
mwPorod101.0—kDa
porod_volumePorod163.0—ų
rgGuinier4.8670.663Å
rgP(r)4.87—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

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 HEPES, 250 mM NaCl, 250 mM KClBuffer concentration—
pH8.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2022-03-22Storage / measurement temperature4.0 / 4.0
Exposure time7200.0Frames3
Wavelength0.1542Sample-to-detector distance0.491
SourceX-ray in houseDetectorRigaku PSAXS Nano
Facility / beamlineYale University / Rigaku MicroMax-007HF · New Haven, United States
q range0.07 – 5.008Sample 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

CategoryFileStatusSizeChecksumDownload and View
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pddfsasbdb/entries/v4/sasdxv4/source/SASDXV4.outdownloaded27489e610c60ca50c66deb1b24b5db3383e2c5074febb09084f822757eed49897cffaDownloadView source fileSource site
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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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sascif:source record
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summary: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:129 field values
Field pathRaw value
codeSASDXV4
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleThe role of kinase domain dimerization in EGFR activation
project.publicationnull
project.statusreleased
project.submitted_date2025-03-16
project.released_date2025-11-02
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDXV4.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDXV4.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXV4_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXV4_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDXV4_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXV4_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDXV4.sascif
experiment.instrument.detector.typeRigaku HyPix - 3000
experiment.instrument.detector.nameRigaku PSAXS Nano
experiment.instrument.detector.resolution100.0
experiment.instrument.nameYale University
experiment.instrument.cityNew Haven
experiment.instrument.countryUnited States
experiment.instrument.beamline_nameRigaku MicroMax-007HF
experiment.instrument.beam_geometrynull
experiment.instrument.type_of_sourceX-ray in house
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_nameReceptor protein-tyrosine kinase (duplication mutant)
experiment.sample.molecule[0].short_nameKDD
experiment.sample.molecule[0].sequenceHHHHHHSSGVDLGTENLYFQSMGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLLVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQG
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeQ504U8
experiment.sample.molecule[0].uniprot_range_first651
experiment.sample.molecule[0].uniprot_range_last993
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEV VLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALA VLSNYDANKTGLKELPMRNLQGQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRG KSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKY SFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEF KDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFL LIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISG NKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVS CRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHY IDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPS IATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLR ILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYV MASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGM NYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALES ILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYM IMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEE DMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSF LQRYSSDPTGALTEDSIDDTFLPVPGEWLVWKQSCSSTSSTHSAAASLQCPSQVLPPASP EGETVADLQTQ
experiment.sample.molecule[0].mw79.594
experiment.sample.molecule[0].total_mw79.594
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_descriptionEGFR kinase domain duplication mutant. The purified construct consists of amino acids 643-976 appended to amino acids 651-993 using mature protein numbering (UniProt Q504U8 numbering: 651-993 followed by a duplicated 643-977 region). The protein construct used for SAXS contains an additional N-terminal non-native 22 amino acid extension and polyhistidine tag (HHHHHHSSGVDLGTENLYFQSM).
experiment.sample.buffer.name20 mM HEPES, 250 mM NaCl, 250 mM KCl
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.nameEGFR kinase domain duplication mutant (KDD) at 2.6 mg/ml
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].addressNew Haven, CT, USA
experiment.contributor[0].affiliation[0].full_nameYale University
experiment.contributor[0].affiliation[0].webpagehttps://www.yale.edu/
experiment.contributor[0].contributor_nameZaritza
experiment.contributor[0].contributor_surnamePetrova
experiment.contributor[0].orcidhttps://orcid.org/0000-0002-4877-4676
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2022-03-22
experiment.storage_temperature4.0
experiment.cell_temperature4.0
experiment.exposure_time7200.0
experiment.number_of_frames3
experiment.wavelength0.1542
experiment.sample_detector_distance0.491
experiment.concentration_minnull
experiment.concentration_max2.6
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.07
experiment.s_max5.008
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionSAXS data from solutions of EGFR kinase domain duplication mutant in 20 mM HEPES, 250 mM NaCl, 250 mM KCl, pH 8 were collected on the Rigaku MicroMax-007HF instrument (Yale University, New Haven, United States) using a Rigaku PSAXS Nano detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.1542 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.60 mg/ml was measured at 4°C. Three successive 7200 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_mw86.0
experimental_mw_errornull
guinier_i0_mw86.0
guinier_i0_mw_errornull
porod_mw101.0
porod_mw_errornull
pddf_i00.2736
pddf_i0_errornull
guinier_i00.278134
guinier_i0_errornull
pddf_rg4.87
pddf_rg_errornull
guinier_rg4.867
guinier_rg_error0.663
pddf_dmax16.4
pddf_dmax_errornull
porod_volume163.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first2
guinier_point_last25
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDXV4_datloglog_img.png
symmetrynull
last_modified2025-11-02T21:11:43.418457+01:00
bragg_peak[]
manifest.json:34 field values
Field pathRaw value
codeSASDXV4
statussuccess
started_at2026-08-11T14:32:37.719435+00:00
finished_at2026-08-11T14:32:44.789741+00:00
source_last_modified2025-11-02T21:11:43.418457+01:00
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View the complete summary.json source
{
  "code": "SASDXV4",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "The role of kinase domain dimerization in EGFR activation",
    "publication": null,
    "status": "released",
    "submitted_date": "2025-03-16",
    "released_date": "2025-11-02"
  },
  "pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDXV4.out",
  "intensities_data": "https://www.sasbdb.org/media/intensities_files/SASDXV4.dat",
  "intensities_log_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXV4_dat_img.png",
  "intensities_kratky_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXV4_kratky_img.png",
  "pddf_plot": "https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDXV4_pofr_img.png",
  "intensities_guinier_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXV4_guinier_img.png",
  "sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDXV4.sascif",
  "experiment": {
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        "type": "Rigaku HyPix - 3000",
        "name": "Rigaku PSAXS Nano",
        "resolution": 100.0
      },
      "name": "Yale University",
      "city": "New Haven",
      "country": "United States",
      "beamline_name": "Rigaku MicroMax-007HF",
      "beam_geometry": null,
      "type_of_source": "X-ray in house",
      "point_source": null,
      "line_collimation": null,
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    "sample": {
      "molecule": [
        {
          "long_name": "Receptor protein-tyrosine kinase (duplication mutant)",
          "short_name": "KDD",
          "sequence": "HHHHHHSSGVDLGTENLYFQSMGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLLVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQG",
          "organism": "Homo sapiens",
          "uniprot_code": "Q504U8",
          "uniprot_range_first": 651,
          "uniprot_range_last": 993,
          "oligomerization": "monomer",
          "molecular_type": "protein",
          "uniprot_sequence": "MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEV\nVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALA\nVLSNYDANKTGLKELPMRNLQGQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRG\nKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKY\nSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEF\nKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFL\nLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISG\nNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVS\nCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHY\nIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPS\nIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLR\nILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYV\nMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGM\nNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALES\nILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYM\nIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEE\nDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSF\nLQRYSSDPTGALTEDSIDDTFLPVPGEWLVWKQSCSSTSSTHSAAASLQCPSQVLPPASP\nEGETVADLQTQ",
          "mw": 79.594,
          "total_mw": 79.594,
          "number_molecules": 1,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": "EGFR kinase domain duplication mutant. The purified construct consists of amino acids 643-976 appended to amino acids 651-993 using mature protein numbering (UniProt Q504U8 numbering: 651-993 followed by a duplicated 643-977 region). The protein construct used for SAXS contains an additional N-terminal non-native 22 amino acid extension and polyhistidine tag (HHHHHHSSGVDLGTENLYFQSM)."
        }
      ],
      "buffer": {
        "name": "20 mM HEPES, 250 mM NaCl, 250 mM KCl",
        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 8.0,
        "deuteration": null
      },
      "purity_method": null,
      "name": "EGFR kinase domain duplication mutant (KDD) at 2.6 mg/ml",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": null,
            "address": "New Haven, CT, USA",
            "full_name": "Yale University",
            "webpage": "https://www.yale.edu/"
          }
        ],
        "contributor_name": "Zaritza",
        "contributor_surname": "Petrova",
        "orcid": "https://orcid.org/0000-0002-4877-4676"
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2022-03-22",
    "storage_temperature": 4.0,
    "cell_temperature": 4.0,
    "exposure_time": 7200.0,
    "number_of_frames": 3,
    "wavelength": 0.1542,
    "sample_detector_distance": 0.491,
    "concentration_min": null,
    "concentration_max": 2.6,
    "sample_volume": null,
    "flow_rate": null,
    "s_min": 0.07,
    "s_max": 5.008,
    "total_exposure_time": null,
    "seccolumn": null
  },
  "fits": [],
  "estimated_volume_method": null,
  "pddf_software": "ATSAS GNOM",
  "pddf_software_version": "5.0",
  "i0_calibration_standard": null,
  "description": null,
  "experiment_description": "SAXS data from solutions of EGFR kinase domain duplication mutant in 20 mM HEPES, 250 mM NaCl, 250 mM KCl, pH 8 were collected on the Rigaku MicroMax-007HF instrument (Yale University, New Haven, United States) using a Rigaku PSAXS Nano detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.1542 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.60 mg/ml was measured at 4°C. Three successive 7200 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_unit": "arbitrary",
  "experimental_mw": 86.0,
  "experimental_mw_error": null,
  "guinier_i0_mw": 86.0,
  "guinier_i0_mw_error": null,
  "porod_mw": 101.0,
  "porod_mw_error": null,
  "pddf_i0": 0.2736,
  "pddf_i0_error": null,
  "guinier_i0": 0.278134,
  "guinier_i0_error": null,
  "pddf_rg": 4.87,
  "pddf_rg_error": null,
  "guinier_rg": 4.867,
  "guinier_rg_error": 0.663,
  "pddf_dmax": 16.4,
  "pddf_dmax_error": null,
  "porod_volume": 163.0,
  "porod_volume_error": null,
  "estimated_volume": null,
  "estimated_volume_error": null,
  "guinier_point_first": 2,
  "guinier_point_last": 25,
  "pddf_point_first": null,
  "pddf_point_last": null,
  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDXV4_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2025-11-02T21:11:43.418457+01:00",
  "bragg_peak": []
}
View the complete manifest.json source
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  "finished_at": "2026-08-11T14:32:44.789741+00:00",
  "source_last_modified": "2025-11-02T21:11:43.418457+01:00",
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