SASDVH4

Human Codanin1 C-terminal domain (frames 779 - 791)

Data type: SASBDB experimental data Status: Published Curve type: SEC-SAS Last updated: 2026-02-02T14:39:37.018334+01:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Human Codanin1 C-terminal domain (frames 779 - 791)

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
Codanin-1
View sequence
SGAARGERRGCSRACEHHAPLPSHLISEIKDVLSLAVGPRDPDEGVSPEHLEQLLGQLGQTLRCRQFLCPPAEQHLAKCSVELASLLVADQIPILGPPAQYRLERGQARRLLHMLLSLWKEDFQGPVPLQLLLSPRNVGLLADTRPREWDLLLFLLRELVEKGLMGRMEIEACLGSLHQAQWPGDFAEELATLSNLFLAEPHLPEPQLRACELVQPNRGTVLAQS
proteinHomo sapiensQ8IWY91005–1227monomerMolecule count 124.961 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11534[3]0.02595352–4.43393 1/nmHas uncertainty columnMissing 06sasbdb/entries/h4/sasdvh4/source/SASDVH4.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)9.3—nm
i0Guinier3670.74—arbitrary
i0P(r)3682.04.71arbitrary
mwExperimental30.0—kDa
mwPorod30.1—kDa
porod_volumePorod51.4—nm³
rgGuinier2.5120.005nm
rgP(r)2.5810.01nm

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 temperature4.0 / 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
codeSASDVH4
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_nameCodanin-1
experiment.sample.molecule[0].short_nameCodanin1
experiment.sample.molecule[0].sequenceSGAARGERRGCSRACEHHAPLPSHLISEIKDVLSLAVGPRDPDEGVSPEHLEQLLGQLGQTLRCRQFLCPPAEQHLAKCSVELASLLVADQIPILGPPAQYRLERGQARRLLHMLLSLWKEDFQGPVPLQLLLSPRNVGLLADTRPREWDLLLFLLRELVEKGLMGRMEIEACLGSLHQAQWPGDFAEELATLSNLFLAEPHLPEPQLRACELVQPNRGTVLAQS
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeQ8IWY9
experiment.sample.molecule[0].uniprot_range_first1005
experiment.sample.molecule[0].uniprot_range_last1227
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMAAVLESLLREEVSVAAVVRWIARSTQGSEDNAGEAAALSSLRALRKEFVPFLLNFLREQ SSRVLPQGPPTPAKTPGASAALPGRPGGPPRGSRGARSQLFPPTEAQSTAAEAPLARRGG RRRGPGPARERGGRGLEEGVSGESLPGAGGRRLRGSGSPSRPSLTLSDPPNLSNLEEFPP VGSVPPGPTGTKPSRRINPTPVSEERSLSKPKTCFTSPPISCVPSSQPSALDTSPWGLGL PPGCRSLQEEREMLRKERSKQLQQSPTPTCPTPELGSPLPSRTGSLTDEPADPARVSSRQ RLELVALVYSSCIAENLVPNLFLELFFVFQLLTARRMVTAKDSDPELSPAVLDSLESPLF QSIHDCVFFAVQVLECHFQVLSNLDKGTLKLLAENERLLCFSPALQGRLRAAYEGSVAKV SLVMPPSTQAVSFQPETDNRANFSSDRAFHTFKKQRDVFYEVLREWEDHHEEPGWDFEKG LGSRIRAMMGQLSAACSHSHFVRLFQKQLLQMCQSPGGAGGTVLGEAPDVLSMLGADKLG RLWRLQERLMAPQSSGGPCPPPTFPGCQGFFRDFILSASSFQFNQHLMDSLSLKIQELNG LALPQHEPNDEDGESDVDWQGERKQFAVVLLSLRLLAKFLGFVAFLPYRGPEPPPTGELQ DSILALRSQVPPVLDVRTLLQRGLQARRAVLTVPWLVEFLSFADHVVPLLEYYRDIFTLL LRLHRSLVLSQESEGKMCFLNKLLLLAVLGWLFQIPTVPEDLFFLEEGPSYAFEVDTVAP EHGLDNAPVVDQQLLYTCCPYIGELRKLLASWVSGSSGRSGGFMRKITPTTTTSLGAQPS QTSQGLQAQLAQAFFHNQPPSLRRTVEFVAERIGSNCVKHIKATLVADLVRQAESLLQEQ LVTQGEEGGDPAQLLEILCSQLCPHGAQALALGREFCQRKSPGAVRALLPEETPAAVLSS AENIAVGLATEKACAWLSANITALIRREVKAAVSRTLRAQGPEPAARGERRGCSRACEHH APLPSHLISEIKDVLSLAVGPRDPDEGVSPEHLEQLLGQLGQTLRCRQFLCPPAEQHLAK CSVELASLLVADQIPILGPPAQYRLERGQARRLLHMLLSLWKEDFQGPVPLQLLLSPRNV GLLADTRPREWDLLLFLLRELVEKGLMGRMEIEACLGSLHQAQWPGDFAEELATLSNLFL AEPHLPEPQLRACELVQPNRGTVLAQS
experiment.sample.molecule[0].mw24.961
experiment.sample.molecule[0].total_mw24.961
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 spans the C-terminal domain, with an additional two non-native amino acids at the N-terminus of the construct (SG).
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 Codanin1 C-terminal domain (frames 779 - 791)
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_temperature4.0
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
experiment.sample_volume45.0
experiment.flow_rate0.3
experiment.s_min0.026
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experiment.total_exposure_timenull
experiment.seccolumn2
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fits[0].chi_square_value2.004
fits[0].p_value0.0
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fits[0].description
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fits[1].chi_square_value40.116
fits[1].p_value0.0
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fits[1].software_version3.2.1
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 Codanin1 Cterm 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. 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 13 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 Codanin1 Cterm is around 25 kDa. MALDI-TOF mass spectrometry suggests a MW 24 965 Da for the Codanin1 Cterm monomer. The MW estimation from the SAXS data (primusqt) varied depending on the method used: Qp = 30.1 kDa, MoW = 30.8 kDa, Vc = 30.6 kDa, Size & Shape = 35.7 kDa (Bayesian Inference MW, 31.7 kDa in the 93% credibility interval of 29.3-32.8 kDa). The models displayed in this entry included: Top: The Alphafold2 predicted model of Codanin1 Cterm monomer compared with the SAXS data using CRYSOL. Bottom: The Alphafold2 predicted model of Codanin1 Cterm dimer compared with the SAXS data using CRYSOL.
tags[]
intensity_unitarbitrary
experimental_mw30.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw30.1
porod_mw_errornull
pddf_i03682.0
pddf_i0_error4.71
guinier_i03670.74
guinier_i0_errornull
pddf_rg2.581
pddf_rg_error0.01
guinier_rg2.512
guinier_rg_error0.005
pddf_dmax9.3
pddf_dmax_errornull
porod_volume51.4
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first15
guinier_point_last168
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDVH4_datloglog_img.png
symmetrynull
last_modified2026-02-02T14:39:37.018334+01:00
bragg_peak[]
manifest.json:34 field values
Field pathRaw value
codeSASDVH4
statussuccess
started_at2026-08-11T16:42:59.897926+00:00
finished_at2026-08-11T16:43:10.884350+00:00
source_last_modified2026-02-02T14:39:37.018334+01:00
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View the complete summary.json source
{
  "code": "SASDVH4",
  "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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      "country": "Germany",
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          "long_name": "Codanin-1",
          "short_name": "Codanin1",
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          "organism": "Homo sapiens",
          "uniprot_code": "Q8IWY9",
          "uniprot_range_first": 1005,
          "uniprot_range_last": 1227,
          "oligomerization": "monomer",
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          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": "The protein construct used for SAXS spans the C-terminal domain, with an additional two non-native amino acids at the N-terminus of the construct (SG)."
        }
      ],
      "buffer": {
        "name": "20 mM Tris HCl, 150 mM NaCl, 5% glycerol",
        "concentration_unit": null,
        "comment": null,
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        "concentration": null,
        "pka": null,
        "ph": 8.0,
        "deuteration": null
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      "purity_method": null,
      "name": "Human Codanin1 C-terminal domain (frames 779 - 791)",
      "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": 4.0,
    "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,
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    "s_max": 4.434,
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    "seccolumn": 2
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    {
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        {
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          "software": "AlphaFold",
          "pdb_link": [],
          "model_title": null,
          "type_of_model": "atomic",
          "software_version": "2.0",
          "model_data": "https://www.sasbdb.org/media/pdb_file/SASDVH4_fit1_model1.pdb",
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          "bead_radius": null,
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          "comment": null,
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      "fit_unit": "1/A",
      "fit_plot": "https://www.sasbdb.org/media/fitting_files/scattering_plots/SASDVH4_fit1_fixed_fit_img.png",
      "software": "CRYSOL",
      "chi_square_value": 2.004,
      "p_value": 0.0,
      "fit_residual_plot": "SASDVH4_fit1_fitresiduals_img.png",
      "fit_data": "https://www.sasbdb.org/media/fitting_files/SASDVH4_fit1.fit",
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      "description": ""
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    {
      "models": [
        {
          "model_plot": "https://www.sasbdb.org/media/pdb_file/images/SASDVH4_fit2_model1_img.png",
          "software": "AlphaFold",
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      "fit_log": "https://www.sasbdb.org/media/fitting_files/log_files/best_6bsec_Codanin1_Cterm_secondP_cut_Codanin1_Cterm_dimer_long.log",
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  "description": null,
  "experiment_description": "The SEC-SAXS data from the solution of Codanin1 Cterm 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. 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 13 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 Codanin1 Cterm is around 25 kDa. MALDI-TOF mass spectrometry suggests a MW 24 965 Da for the Codanin1 Cterm monomer. The MW estimation from the SAXS data (primusqt) varied depending on the method used: Qp = 30.1 kDa, MoW = 30.8 kDa, Vc = 30.6 kDa, Size & Shape = 35.7 kDa (Bayesian Inference MW, 31.7 kDa in the 93% credibility interval of 29.3-32.8 kDa). The models displayed in this entry included: Top: The Alphafold2 predicted model of Codanin1 Cterm monomer compared with the SAXS data using CRYSOL. Bottom: The Alphafold2 predicted model of Codanin1 Cterm dimer compared with the SAXS data using CRYSOL.",
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  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDVH4_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2026-02-02T14:39:37.018334+01:00",
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}
View the complete manifest.json source
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