SASDV39

Human CDAN1-interacting nuclease 1 (frames 692 - 701)

Data type: SASBDB experimental data Status: Published Curve type: SEC-SAS Last updated: 2026-02-02T14:39:25.988588+01:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Human CDAN1-interacting nuclease 1 (frames 692 - 701)

Concentration— – 10.0 Buffer / pH20 mM Tris HCl, 150 mM NaCl, 5% glycerol / 8.0
Experimental temperature20.0 Facility / beamlinePETRA III / EMBL P12
Wavelength0.123982 nmExposure0.495 s × 1200

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
CDAN1-interacting nuclease 1
View sequence
SGTLPETGSSEAMILTKAQYDEIAQCLVSVPPTRQSLRKLKQRFPSQSQATLLSIFSQEYQKHIKRTHAKHHTSEAIESYYQRYLNGVVKNGAAPVLLDLANEVDYAPSLMARLILERFLQEHEETPPSKSIINSMLRDPSQIPDGVLANQVYQCIVNDCCYGPLVDCIKHAIGHEHEVLLRDLLLEKNLSFLDEDQLRAKGYDKTPDFILQVPVAVEGHIIHWIESKASFGDECSHHAYLHDQFWSYWNRFGPGLVIYWYGFIQELDCNRERGILLKACFPTNIVTLCHSIA
proteinHomo sapiensQ9Y2V01–281monomerMolecule count 133.381 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11534[3]0.02595352–4.43393 1/nmHas uncertainty columnMissing 0238sasbdb/entries/39/sasdv39/source/SASDV39.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)8.94—nm
i0Guinier2016.77—arbitrary
i0P(r)2022.08.77arbitrary
mwExperimental33.0—kDa
mwPorod62.0—kDa
porod_volumePorod104.0—nm³
rgGuinier2.810.033nm
rgP(r)2.8160.01nm

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 HCl, 150 mM NaCl, 5% glycerolBuffer concentration—
pH8.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2023-09-29Storage / measurement temperature20.0 / 20.0
Exposure time0.495Frames1200
Wavelength0.123982Sample-to-detector distance3.0
SourceX-ray synchrotronDetectorPilatus 6M
Facility / beamlinePETRA III / EMBL P12 · DESY; Hamburg, Germany
q range0.026 – 4.434Sample volume / flow rate45.0 / 0.3

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:179 field values
Field pathRaw value
codeSASDV39
statusPublished
type_of_curveSEC-SAS
angular_unit1/nm
project.titleAnemia-associated mutations disrupt the CDIN1-Codanin1 complex in inherited congenital dyserythropoietic anemia I (CDA-I) disease.
project.publication.titleAnemia-associated mutations disrupt the CDIN1-Codanin1 complex in inherited congenital dyserythropoietic anemia I (CDA-I) disease.
project.publication.author_listStojaspal M, Brom T, Nečasová I, Janovič T, Veverka P, Verma N, Uhrík L, Hernychova L, Hofr C
project.publication.journalFEBS J
project.publication.doi10.1111/febs.70421
project.publication.pmid41609415
project.publication.published_date2026 Jan 29
project.statusreleased
project.submitted_date2024-07-10
project.released_date2026-02-02
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experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus 6M
experiment.instrument.detector.resolutionnull
experiment.instrument.namePETRA III
experiment.instrument.cityDESY; Hamburg
experiment.instrument.countryGermany
experiment.instrument.beamline_nameEMBL P12
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_nameCDAN1-interacting nuclease 1
experiment.sample.molecule[0].short_nameCDIN1
experiment.sample.molecule[0].sequenceSGTLPETGSSEAMILTKAQYDEIAQCLVSVPPTRQSLRKLKQRFPSQSQATLLSIFSQEYQKHIKRTHAKHHTSEAIESYYQRYLNGVVKNGAAPVLLDLANEVDYAPSLMARLILERFLQEHEETPPSKSIINSMLRDPSQIPDGVLANQVYQCIVNDCCYGPLVDCIKHAIGHEHEVLLRDLLLEKNLSFLDEDQLRAKGYDKTPDFILQVPVAVEGHIIHWIESKASFGDECSHHAYLHDQFWSYWNRFGPGLVIYWYGFIQELDCNRERGILLKACFPTNIVTLCHSIA
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeQ9Y2V0
experiment.sample.molecule[0].uniprot_range_first1
experiment.sample.molecule[0].uniprot_range_last281
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMILTKAQYDEIAQCLVSVPPTRQSLRKLKQRFPSQSQATLLSIFSQEYQKHIKRTHAKHH TSEAIESYYQRYLNGVVKNGAAPVLLDLANEVDYAPSLMARLILERFLQEHEETPPSKSI INSMLRDPSQIPDGVLANQVYQCIVNDCCYGPLVDCIKHAIGHEHEVLLRDLLLEKNLSF LDEDQLRAKGYDKTPDFILQVPVAVEGHIIHWIESKASFGDECSHHAYLHDQFWSYWNRF GPGLVIYWYGFIQELDCNRERGILLKACFPTNIVTLCHSIA
experiment.sample.molecule[0].mw33.381
experiment.sample.molecule[0].total_mw33.381
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_descriptionThe protein construct used for SAXS contains an additional 12 non-native amino acids at the N-terminus (SGTLPETGSSEA).
experiment.sample.buffer.name20 mM Tris HCl, 150 mM NaCl, 5% glycerol
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.nameHuman CDAN1-interacting nuclease 1 (frames 692 - 701)
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].addressnull
experiment.contributor[0].affiliation[0].full_nameNational Centre for Biomolecular Research, Faculty of Science, Masaryk University
experiment.contributor[0].affiliation[0].webpagenull
experiment.contributor[0].contributor_nameTomas
experiment.contributor[0].contributor_surnameBrom
experiment.contributor[0].orcidhttps://orcid.org/0000-0003-1046-192X
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2023-09-29
experiment.storage_temperature20.0
experiment.cell_temperature20.0
experiment.exposure_time0.495
experiment.number_of_frames1200
experiment.wavelength0.123982
experiment.sample_detector_distance3.0
experiment.concentration_minnull
experiment.concentration_max10.0
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experiment.flow_rate0.3
experiment.s_min0.026
experiment.s_max4.434
experiment.total_exposure_timenull
experiment.seccolumn2
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fits[0].p_value0.3057
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fits[1].p_value0.0
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fits[1].description
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionThe SEC-SAXS data from the solution of CDIN1 diluted in 20 mM Tris HCl, 150 mM NaCl, 5% glycerol, pH 8.0 buffer were collected on the EMBL P12 beamline at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.123982 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAXS was employed. The sample (45 μl at 10 mg/ml) was injected and ran into a GE Superdex 200 Increase 5/150 column at a flow rate of 0.3 ml/min at 20°C. Scattering data were collected throughout the entire SEC column elution with an exposure time of 0.495 sec/frame (for 1200 frames total). The data were normalized to the intensity of the transmitted beam. The selected area of sample elution peak was selected and processed (averaged and buffer subtracted) from 10 data frames using CHROMIXS and primusqt from the ATSAS 3.2.1 package. The radius of gyration (Rg), forward scattering (I(0)), maximum particle dimension (Dmax), and the distance distribution function were determined using primusqt and GNOM. The calculated molecular weight (MW) of CDIN1 is around 67 kDa. MALDI-TOF mass spectrometry suggests a MW 33 369 Da for the CDIN1 monomer. The MW estimation from the SAXS data (primusqt) varied depending on the method used: Qp = 66.3 kDa, MoW = 62.3 kDa, Vc = 66.6 kDa, Size & Shape = 76.6 kDa (Bayesian Inference MW, 62.3 kDa in the 92% credibility interval of 58.8-67.9 kDa). The models displayed in this entry included: Top: The Alphafold2 predicted model of CDIN1 dimer compared with the SAXS data using CRYSOL. Bottom: The Alphafold2 predicted model of CDIN1 monomer compared with the SAXS data using CRYSOL.
tags[]
intensity_unitarbitrary
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experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
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porod_mw_errornull
pddf_i02022.0
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guinier_i02016.77
guinier_i0_errornull
pddf_rg2.816
pddf_rg_error0.01
guinier_rg2.81
guinier_rg_error0.033
pddf_dmax8.94
pddf_dmax_errornull
porod_volume104.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first45
guinier_point_last148
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDV39_datloglog_img.png
symmetrynull
last_modified2026-02-02T14:39:25.988588+01:00
bragg_peak[]
manifest.json:34 field values
Field pathRaw value
codeSASDV39
statussuccess
started_at2026-08-11T16:38:33.687462+00:00
finished_at2026-08-11T16:38:42.059102+00:00
source_last_modified2026-02-02T14:39:25.988588+01:00
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View the complete summary.json source
{
  "code": "SASDV39",
  "status": "Published",
  "type_of_curve": "SEC-SAS",
  "angular_unit": "1/nm",
  "project": {
    "title": "Anemia-associated mutations disrupt the CDIN1-Codanin1 complex in inherited congenital dyserythropoietic anemia I (CDA-I) disease.",
    "publication": {
      "title": "Anemia-associated mutations disrupt the CDIN1-Codanin1 complex in inherited congenital dyserythropoietic anemia I (CDA-I) disease.",
      "author_list": "Stojaspal M, Brom T, Nečasová I, Janovič T, Veverka P, Verma N, Uhrík L, Hernychova L, Hofr C",
      "journal": "FEBS J",
      "doi": "10.1111/febs.70421",
      "pmid": "41609415",
      "published_date": "2026 Jan 29"
    },
    "status": "released",
    "submitted_date": "2024-07-10",
    "released_date": "2026-02-02"
  },
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      },
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      "country": "Germany",
      "beamline_name": "EMBL P12",
      "beam_geometry": null,
      "type_of_source": "X-ray synchrotron",
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    },
    "sample": {
      "molecule": [
        {
          "long_name": "CDAN1-interacting nuclease 1",
          "short_name": "CDIN1",
          "sequence": "SGTLPETGSSEAMILTKAQYDEIAQCLVSVPPTRQSLRKLKQRFPSQSQATLLSIFSQEYQKHIKRTHAKHHTSEAIESYYQRYLNGVVKNGAAPVLLDLANEVDYAPSLMARLILERFLQEHEETPPSKSIINSMLRDPSQIPDGVLANQVYQCIVNDCCYGPLVDCIKHAIGHEHEVLLRDLLLEKNLSFLDEDQLRAKGYDKTPDFILQVPVAVEGHIIHWIESKASFGDECSHHAYLHDQFWSYWNRFGPGLVIYWYGFIQELDCNRERGILLKACFPTNIVTLCHSIA",
          "organism": "Homo sapiens",
          "uniprot_code": "Q9Y2V0",
          "uniprot_range_first": 1,
          "uniprot_range_last": 281,
          "oligomerization": "monomer",
          "molecular_type": "protein",
          "uniprot_sequence": "MILTKAQYDEIAQCLVSVPPTRQSLRKLKQRFPSQSQATLLSIFSQEYQKHIKRTHAKHH\nTSEAIESYYQRYLNGVVKNGAAPVLLDLANEVDYAPSLMARLILERFLQEHEETPPSKSI\nINSMLRDPSQIPDGVLANQVYQCIVNDCCYGPLVDCIKHAIGHEHEVLLRDLLLEKNLSF\nLDEDQLRAKGYDKTPDFILQVPVAVEGHIIHWIESKASFGDECSHHAYLHDQFWSYWNRF\nGPGLVIYWYGFIQELDCNRERGILLKACFPTNIVTLCHSIA",
          "mw": 33.381,
          "total_mw": 33.381,
          "number_molecules": 1,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": "The protein construct used for SAXS contains an additional 12 non-native amino acids at the N-terminus (SGTLPETGSSEA)."
        }
      ],
      "buffer": {
        "name": "20 mM Tris HCl, 150 mM NaCl, 5% glycerol",
        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 8.0,
        "deuteration": null
      },
      "purity_method": null,
      "name": "Human CDAN1-interacting nuclease 1 (frames 692 - 701)",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": null,
            "address": null,
            "full_name": "National Centre for Biomolecular Research, Faculty of Science, Masaryk University",
            "webpage": null
          }
        ],
        "contributor_name": "Tomas",
        "contributor_surname": "Brom",
        "orcid": "https://orcid.org/0000-0003-1046-192X"
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2023-09-29",
    "storage_temperature": 20.0,
    "cell_temperature": 20.0,
    "exposure_time": 0.495,
    "number_of_frames": 1200,
    "wavelength": 0.123982,
    "sample_detector_distance": 3.0,
    "concentration_min": null,
    "concentration_max": 10.0,
    "sample_volume": 45.0,
    "flow_rate": 0.3,
    "s_min": 0.026,
    "s_max": 4.434,
    "total_exposure_time": null,
    "seccolumn": 2
  },
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    {
      "models": [
        {
          "model_plot": "https://www.sasbdb.org/media/pdb_file/images/SASDV39_fit1_model1_img.png",
          "software": "AlphaFold",
          "pdb_link": [],
          "model_title": null,
          "type_of_model": "atomic",
          "software_version": "2.0",
          "model_data": "https://www.sasbdb.org/media/pdb_file/SASDV39_fit1_model1.pdb",
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          "bead_radius": null,
          "log": null,
          "symmetry": null,
          "comment": null,
          "user": 720
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      "fit_unit": "1/A",
      "fit_plot": "https://www.sasbdb.org/media/fitting_files/scattering_plots/SASDV39_fit1_fixed_fit_img.png",
      "software": "CRYSOL",
      "chi_square_value": 1.063,
      "p_value": 0.3057,
      "fit_residual_plot": "SASDV39_fit1_fitresiduals_img.png",
      "fit_data": "https://www.sasbdb.org/media/fitting_files/SASDV39_fit1.FIT",
      "fit_log": "https://www.sasbdb.org/media/fitting_files/log_files/CHROMI2.LOG",
      "software_version": "3.2.1",
      "description": ""
    },
    {
      "models": [
        {
          "model_plot": "https://www.sasbdb.org/media/pdb_file/images/SASDV39_fit2_model1_img.png",
          "software": "AlphaFold",
          "pdb_link": [],
          "model_title": null,
          "type_of_model": "atomic",
          "software_version": "2.0",
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      "fit_unit": "1/A",
      "fit_plot": "https://www.sasbdb.org/media/fitting_files/scattering_plots/SASDV39_fit2_fixed_fit_img.png",
      "software": "CRYSOL",
      "chi_square_value": 2.596,
      "p_value": 0.0,
      "fit_residual_plot": "SASDV39_fit2_fitresiduals_img.png",
      "fit_data": "https://www.sasbdb.org/media/fitting_files/SASDV39_fit2.FIT",
      "fit_log": "https://www.sasbdb.org/media/fitting_files/log_files/CHROMI1.LOG",
      "software_version": "3.2.1.",
      "description": ""
    }
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  "estimated_volume_method": null,
  "pddf_software": "ATSAS GNOM",
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  "i0_calibration_standard": null,
  "description": null,
  "experiment_description": "The SEC-SAXS data from the solution of CDIN1 diluted in 20 mM Tris HCl, 150 mM NaCl, 5% glycerol, pH 8.0 buffer were collected on the EMBL P12 beamline at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.123982 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAXS was employed. The sample (45 μl at 10 mg/ml) was injected and ran into a GE Superdex 200 Increase 5/150 column at a flow rate of 0.3 ml/min at 20°C. Scattering data were collected throughout the entire SEC column elution with an exposure time of 0.495 sec/frame (for 1200 frames total). The data were normalized to the intensity of the transmitted beam. The selected area of sample elution peak was selected and processed (averaged and buffer subtracted) from 10 data frames using CHROMIXS and primusqt from the ATSAS 3.2.1 package. The radius of gyration (Rg), forward scattering (I(0)), maximum particle dimension (Dmax), and the distance distribution function were determined using primusqt and GNOM. The calculated molecular weight (MW) of CDIN1 is around 67 kDa. MALDI-TOF mass spectrometry suggests a MW 33 369 Da for the CDIN1 monomer. The MW estimation from the SAXS data (primusqt) varied depending on the method used: Qp = 66.3 kDa, MoW = 62.3 kDa, Vc = 66.6 kDa, Size & Shape = 76.6 kDa (Bayesian Inference MW, 62.3 kDa in the 92% credibility interval of 58.8-67.9 kDa). The models displayed in this entry included: Top: The Alphafold2 predicted model of CDIN1 dimer compared with the SAXS data using CRYSOL. Bottom: The Alphafold2 predicted model of CDIN1 monomer compared with the SAXS data using CRYSOL.",
  "tags": [],
  "intensity_unit": "arbitrary",
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  "experimental_mw_error": null,
  "guinier_i0_mw": null,
  "guinier_i0_mw_error": null,
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  "porod_mw_error": null,
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  "pddf_i0_error": 8.77,
  "guinier_i0": 2016.77,
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  "pddf_rg": 2.816,
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  "guinier_rg": 2.81,
  "guinier_rg_error": 0.033,
  "pddf_dmax": 8.94,
  "pddf_dmax_error": null,
  "porod_volume": 104.0,
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  "estimated_volume": null,
  "estimated_volume_error": null,
  "guinier_point_first": 45,
  "guinier_point_last": 148,
  "pddf_point_first": null,
  "pddf_point_last": null,
  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDV39_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2026-02-02T14:39:25.988588+01:00",
  "bragg_peak": []
}
View the complete manifest.json source
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