SASDG47

2:4 heterohexamer of pUL7 and pUL51 from herpes simplex virus 1

Data type: SASBDB experimental data Status: Published Curve type: SEC-SAS Last updated: 2023-06-21T07:55:24.740692+02:00

The quoted experimental molecular mass, that corresponds to a 2:4 pUL7:pUL51 heterohexamer, was determined from SEC-MALLS-RI measurements performed in parallel to the SEC-SAXS. The SEC-SAXS data, Rg correlations through the dimer elution peak as well as the the SEC-MALLS-RI data are made available in the full-entry zip archive. The GASBORMX model displayed in this entry represents a 100 % volume fraction of the heterohexamer in solution that has been separated from a 1:2 pUL7:pUL51 heterotrimer (refer to SASBDB entry SASDG57).

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · 2:4 heterohexamer of pUL7 and pUL51 from herpes simplex virus 1

Concentration— – 8.0 Buffer / pH20 mM HEPES, 200 mM NaCl, 3% (v/v) glycerol, 1 mM DTT / 7.5
Experimental temperature20.2 Facility / beamlinePETRA III / EMBL P12
Wavelength0.124 nmExposure0.995 s × 48

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Tegument protein UL7
View sequence
MAAATADDEGSAATILKQAIAGDRSLVEAAEAISQQTLLRLACEVRQVGDRQPRFTATSIARVDVAPGCRLRFVLDGSPEDAYVTSEDYFKRCCGQSSYRGFAVAVLTANEDHVHSLAVPPLVLLHRFSLFNPRDLLDFELACLLMYLENCPRSHATPSTFAKVLAWLGVAGRRTSPFERVRCLFLRSCHWVLNTLMFMVHVKPFDDEFVLPHWYMARYLLANNPPPVLSALFCATPTSSSFRLPGPPPRSDCVAYNPAGIMGSCWASEEVRAPLVYWWLSETPKRQTSSLFYQFCGSLEVLFQ
proteinHuman alphaherpesvirus 1 strain KOSA0A110B4Q71–296dimerMolecule count 233.907 kDa
Tegument protein UL51
View sequence
MASLLGAISGWGARPEEQYEMIRAAVPPSEAEPRLQEALVVVNALLPAPITLDDALGSLDDTRRLVKARALARTYHACMVNLERLARHHPGLEAPTIDGAVAAHQDKMRRLADTCMATILQMYMSVGAADKSADVLVSQAIRSMAESDVVMEDVAIAERALGLSAFGVAGGTRSGGLGVTEAPSLGHPHTPPPEVTLAPAARNGDALPDPKPESCPRVSVPRPTASPTAPRPGPSRAAPCVLGQ
proteinHuman alphaherpesvirus 1 strain KOSD3YPL01–244tetramerMolecule count 425.448 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
12633[3]0.0224526–7.3176 1/nmHas uncertainty columnMissing 0193sasbdb/entries/47/sasdg47/source/SASDG47.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)19.7—nm
i0Guinier3100.167.09arbitrary
i0P(r)3136.0—arbitrary
mwExperimental168.0—kDa
mwPorod103.9—kDa
porod_volumePorod340.0—nm³
rgGuinier4.560.28nm
rgP(r)4.788—nm

These values are reported by SASBDB; SAXSdb did not recalculate them from the experimental curve.

▼

3. Source Fits and Models Source Fits & Models

Fit 1 · DAMMIN 5.3

χ²: 0.91CorMap p: 0.805657Unit: 1/A

Fit of the refined DAMMIN model to the HSV-1 pUL7:pUL51 2:4 heterohexamer SAXS profile

ModelName / TypeSoftwareSymmetryModel MWPDB DeclarationSource file
1—dummyDAMMIN SUPCOMB 23 (r10552)P2207.31—Model Image

Fit 2 · GASBOR 2.3i

χ²: 1.0CorMap p: 0.363345Unit: 1/A

Fit of the representative GASBOR model to the HSV-1 pUL7:pUL51 2:4 heterohexamer SAXS profile

ModelName / TypeSoftwareSymmetryModel MWPDB DeclarationSource file
1—dummyGASBOR 2.3iP2——Model Image
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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, 200 mM NaCl, 3% (v/v) glycerol, 1 mM DTTBuffer concentration—
pH7.5Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2019-05-16Storage / measurement temperature— / 20.2
Exposure time0.995Frames48
Wavelength0.124Sample-to-detector distance3.0
SourceX-ray synchrotronDetectorPilatus 6M
Facility / beamlinePETRA III / EMBL P12 · DESY; Hamburg, Germany
q range0.022 – 7.318Sample volume / flow rate90.0 / 0.5

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:196 field values
Field pathRaw value
codeSASDG47
statusPublished
type_of_curveSEC-SAS
angular_unit1/nm
project.titleInsights into herpesvirus assembly from the structure of the pUL7:pUL51 complex.
project.publication.titleInsights into herpesvirus assembly from the structure of the pUL7:pUL51 complex.
project.publication.author_listButt BG, Owen DJ, Jeffries CM, Ivanova L, Hill CH, Houghton JW, Ahmed MF, Antrobus R, Svergun DI, Welch JJ, Crump CM, Graham SC
project.publication.journalElife
project.publication.doi10.7554/eLife.53789
project.publication.pmid32391791
project.publication.published_date2020 May 11
project.statusreleased
project.submitted_date2019-10-17
project.released_date2020-05-20
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDG47.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDG47.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDG47_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDG47_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDG47_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDG47_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDG47.sascif
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_nameTegument protein UL7
experiment.sample.molecule[0].short_namepUL7
experiment.sample.molecule[0].sequenceMAAATADDEGSAATILKQAIAGDRSLVEAAEAISQQTLLRLACEVRQVGDRQPRFTATSIARVDVAPGCRLRFVLDGSPEDAYVTSEDYFKRCCGQSSYRGFAVAVLTANEDHVHSLAVPPLVLLHRFSLFNPRDLLDFELACLLMYLENCPRSHATPSTFAKVLAWLGVAGRRTSPFERVRCLFLRSCHWVLNTLMFMVHVKPFDDEFVLPHWYMARYLLANNPPPVLSALFCATPTSSSFRLPGPPPRSDCVAYNPAGIMGSCWASEEVRAPLVYWWLSETPKRQTSSLFYQFCGSLEVLFQ
experiment.sample.molecule[0].organismHuman alphaherpesvirus 1 strain KOS
experiment.sample.molecule[0].uniprot_codeA0A110B4Q7
experiment.sample.molecule[0].uniprot_range_first1
experiment.sample.molecule[0].uniprot_range_last296
experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMAAATADDEGSAATILKQAIAGDRSLVEAAEAISQQTLLRLACEVRQVGDRQPRFTATSI ARVDVAPGCRLRFVLDGSPEDAYVTSEDYFKRCCGQSSYRGFAVAVLTANEDHVHSLAVP PLVLLHRFSLFNPRDLLDFELACLLMYLENCPRSHATPSTFAKVLAWLGVAGRRTSPFER VRCLFLRSCHWVLNTLMFMVHVKPFDDEFVLPHWYMARYLLANNPPPVLSALFCATPTSS SFRLPGPPPRSDCVAYNPAGIMGSCWASEEVRAPLVYWWLSETPKRQTSSLFYQFC
experiment.sample.molecule[0].mw33.907
experiment.sample.molecule[0].total_mw67.814
experiment.sample.molecule[0].number_molecules2
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_nameTegument protein UL51
experiment.sample.molecule[1].short_namepUL51
experiment.sample.molecule[1].sequenceMASLLGAISGWGARPEEQYEMIRAAVPPSEAEPRLQEALVVVNALLPAPITLDDALGSLDDTRRLVKARALARTYHACMVNLERLARHHPGLEAPTIDGAVAAHQDKMRRLADTCMATILQMYMSVGAADKSADVLVSQAIRSMAESDVVMEDVAIAERALGLSAFGVAGGTRSGGLGVTEAPSLGHPHTPPPEVTLAPAARNGDALPDPKPESCPRVSVPRPTASPTAPRPGPSRAAPCVLGQ
experiment.sample.molecule[1].organismHuman alphaherpesvirus 1 strain KOS
experiment.sample.molecule[1].uniprot_codeD3YPL0
experiment.sample.molecule[1].uniprot_range_first1
experiment.sample.molecule[1].uniprot_range_last244
experiment.sample.molecule[1].oligomerizationtetramer
experiment.sample.molecule[1].molecular_typeprotein
experiment.sample.molecule[1].uniprot_sequenceMASLLGAICGWGARPEEQYEMIRAAVPPSEAEPRLQEALVVVNALLPAPITLDDALGSLD DTRRLVKARALARTYHACMVNLERLARHHPGLEAPTIDGAVAAHQDKMRRLADTCMATIL QMYMSVGAADKSADVLVSQAIRSMAESDVVMEDVAIAERALGLSAFGVAGGTRSGGLGVT EAPSLGHPHTPPPEVTLAPAARNGDALPDPKPESCPRVSVPRPTASPTAPRPGPSRAAPC VLGQ
experiment.sample.molecule[1].mw25.448
experiment.sample.molecule[1].total_mw101.792
experiment.sample.molecule[1].number_molecules4
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.name20 mM HEPES, 200 mM NaCl, 3% (v/v) glycerol, 1 mM DTT
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.name2:4 heterohexamer of pUL7 and pUL51 from herpes simplex virus 1
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_nameUniversity of Cambridge
experiment.contributor[0].affiliation[0].webpagenull
experiment.contributor[0].contributor_nameBenjamin
experiment.contributor[0].contributor_surnameButt
experiment.contributor[0].orcidhttps://orcid.org/0000-0001-6718-0470
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2019-05-16
experiment.storage_temperaturenull
experiment.cell_temperature20.2
experiment.exposure_time0.995
experiment.number_of_frames48
experiment.wavelength0.124
experiment.sample_detector_distance3.0
experiment.concentration_minnull
experiment.concentration_max8.0
experiment.sample_volume90.0
experiment.flow_rate0.5
experiment.s_min0.022
experiment.s_max7.318
experiment.total_exposure_timenull
experiment.seccolumn1
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fits[0].models[0].softwareDAMMIN
fits[0].models[0].pdb_link[]
fits[0].models[0].model_titlenull
fits[0].models[0].type_of_modeldummy
fits[0].models[0].software_versionSUPCOMB 23 (r10552)
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fits[0].models[0].model_mw207.31
fits[0].models[0].bead_radius3.75
fits[0].models[0].lognull
fits[0].models[0].symmetryP2
fits[0].models[0].commentRefined DAMMIN model of the HSV-1 pUL7:pUL51 2:4 heterohexamer
fits[0].models[0].user502
fits[0].fit_unit1/A
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fits[0].softwareDAMMIN
fits[0].chi_square_value0.91
fits[0].p_value0.805657
fits[0].fit_residual_plotSASDG47_fit1_fitresiduals_img.png
fits[0].fit_datahttps://www.sasbdb.org/media/fitting_files/SASDG47_fit1.fir
fits[0].fit_lognull
fits[0].software_version5.3
fits[0].descriptionFit of the refined DAMMIN model to the HSV-1 pUL7:pUL51 2:4 heterohexamer SAXS profile
fits[1].models[0].model_plothttps://www.sasbdb.org/media/pdb_file/images/SASDG47_fit2_model1_img.png
fits[1].models[0].softwareGASBOR
fits[1].models[0].pdb_link[]
fits[1].models[0].model_titlenull
fits[1].models[0].type_of_modeldummy
fits[1].models[0].software_version2.3i
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fits[1].models[0].model_mwnull
fits[1].models[0].bead_radius1.9
fits[1].models[0].lognull
fits[1].models[0].symmetryP2
fits[1].models[0].commentRepresentative GASBOR model of the HSV-1 pUL7:pUL51 2:4 heterohexamer
fits[1].models[0].user502
fits[1].fit_unit1/A
fits[1].fit_plothttps://www.sasbdb.org/media/fitting_files/scattering_plots/SASDG47_fit2_fixed_fit_img.png
fits[1].softwareGASBOR
fits[1].chi_square_value1.0
fits[1].p_value0.363345
fits[1].fit_residual_plotSASDG47_fit2_fitresiduals_img.png
fits[1].fit_datahttps://www.sasbdb.org/media/fitting_files/SASDG47_fit2.fir
fits[1].fit_lognull
fits[1].software_version2.3i
fits[1].descriptionFit of the representative GASBOR model to the HSV-1 pUL7:pUL51 2:4 heterohexamer SAXS profile
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionThe quoted experimental molecular mass, that corresponds to a 2:4 pUL7:pUL51 heterohexamer, was determined from SEC-MALLS-RI measurements performed in parallel to the SEC-SAXS. The SEC-SAXS data, Rg correlations through the dimer elution peak as well as the the SEC-MALLS-RI data are made available in the full-entry zip archive. The GASBORMX model displayed in this entry represents a 100 % volume fraction of the heterohexamer in solution that has been separated from a 1:2 pUL7:pUL51 heterotrimer (refer to SASBDB entry SASDG57).
experiment_descriptionSynchrotron SAXS data from the 2:4 heterohexamer of pUL7 and pUL51 from herpes simplex virus 1 in 20 mM HEPES, 200 mM NaCl, 3% (v/v) glycerol, 1 mM DTT, pH 7.5 were collected on the EMBL P12 beam line at PETRA III (Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 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 90.00 μl sample at 8 mg/ml was injected at a 0.50 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 20.2°C. 48 successive 0.995 second frames were collected through the minor SEC-elution peak (corresponding to the heterohexamer) and processed using CHROMIXS. 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_mw168.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw103.9
porod_mw_errornull
pddf_i03136.0
pddf_i0_errornull
guinier_i03100.16
guinier_i0_error7.09
pddf_rg4.788
pddf_rg_errornull
guinier_rg4.56
guinier_rg_error0.28
pddf_dmax19.7
pddf_dmax_errornull
porod_volume340.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first21
guinier_point_last95
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDG47_datloglog_img.png
symmetrynull
last_modified2023-06-21T07:55:24.740692+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDG47
statussuccess
started_at2026-08-11T15:21:43.832917+00:00
finished_at2026-08-11T15:22:08.373769+00:00
source_last_modified2023-06-21T07:55:24.740692+02:00
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View the complete summary.json source
{
  "code": "SASDG47",
  "status": "Published",
  "type_of_curve": "SEC-SAS",
  "angular_unit": "1/nm",
  "project": {
    "title": "Insights into herpesvirus assembly from the structure of the pUL7:pUL51 complex.",
    "publication": {
      "title": "Insights into herpesvirus assembly from the structure of the pUL7:pUL51 complex.",
      "author_list": "Butt BG, Owen DJ, Jeffries CM, Ivanova L, Hill CH, Houghton JW, Ahmed MF, Antrobus R, Svergun DI, Welch JJ, Crump CM, Graham SC",
      "journal": "Elife",
      "doi": "10.7554/eLife.53789",
      "pmid": "32391791",
      "published_date": "2020 May 11"
    },
    "status": "released",
    "submitted_date": "2019-10-17",
    "released_date": "2020-05-20"
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      "city": "DESY; Hamburg",
      "country": "Germany",
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      "point_source": null,
      "line_collimation": null,
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          "short_name": "pUL7",
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          "uniprot_code": "A0A110B4Q7",
          "uniprot_range_first": 1,
          "uniprot_range_last": 296,
          "oligomerization": "dimer",
          "molecular_type": "protein",
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          "number_molecules": 2,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
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          "long_name": "Tegument protein UL51",
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          "sequence": "MASLLGAISGWGARPEEQYEMIRAAVPPSEAEPRLQEALVVVNALLPAPITLDDALGSLDDTRRLVKARALARTYHACMVNLERLARHHPGLEAPTIDGAVAAHQDKMRRLADTCMATILQMYMSVGAADKSADVLVSQAIRSMAESDVVMEDVAIAERALGLSAFGVAGGTRSGGLGVTEAPSLGHPHTPPPEVTLAPAARNGDALPDPKPESCPRVSVPRPTASPTAPRPGPSRAAPCVLGQ",
          "organism": "Human alphaherpesvirus 1 strain KOS",
          "uniprot_code": "D3YPL0",
          "uniprot_range_first": 1,
          "uniprot_range_last": 244,
          "oligomerization": "tetramer",
          "molecular_type": "protein",
          "uniprot_sequence": "MASLLGAICGWGARPEEQYEMIRAAVPPSEAEPRLQEALVVVNALLPAPITLDDALGSLD\nDTRRLVKARALARTYHACMVNLERLARHHPGLEAPTIDGAVAAHQDKMRRLADTCMATIL\nQMYMSVGAADKSADVLVSQAIRSMAESDVVMEDVAIAERALGLSAFGVAGGTRSGGLGVT\nEAPSLGHPHTPPPEVTLAPAARNGDALPDPKPESCPRVSVPRPTASPTAPRPGPSRAAPC\nVLGQ",
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          "number_molecules": 4,
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          "deuteration": null,
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          "molecule_description": null
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        "deuteration": null
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      "name": "2:4 heterohexamer of pUL7 and pUL51 from herpes simplex virus 1",
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      "absorbption": null,
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          {
            "short_name": null,
            "address": null,
            "full_name": "University of Cambridge",
            "webpage": null
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        "contributor_name": "Benjamin",
        "contributor_surname": "Butt",
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    "concentration_unit": null,
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}
View the complete manifest.json source
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