SASDG57

1:2 heterotrimer 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 1:2 pUL7:pUL51 heterotrimer, was determined from SEC-MALLS-RI measurements performed in parallel to the SEC-SAXS. The SEC-SAXS data, Rg correlations through the heterotrimer 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 an 80 % volume fraction of the heterotrimer (corresponding fit, top) combined with a 20% volume fraction of a 2:4 pUL7:pUL51 heterohexamer (corresponding fit, bottom), due to incomplete SEC-separation between the two forms of the complex (also refer to SASBDB entry SASDG47).

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · 1:2 heterotrimer 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 × 35

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Tegument protein UL7
View sequence
MAAATADDEGSAATILKQAIAGDRSLVEAAEAISQQTLLRLACEVRQVGDRQPRFTATSIARVDVAPGCRLRFVLDGSPEDAYVTSEDYFKRCCGQSSYRGFAVAVLTANEDHVHSLAVPPLVLLHRFSLFNPRDLLDFELACLLMYLENCPRSHATPSTFAKVLAWLGVAGRRTSPFERVRCLFLRSCHWVLNTLMFMVHVKPFDDEFVLPHWYMARYLLANNPPPVLSALFCATPTSSSFRLPGPPPRSDCVAYNPAGIMGSCWASEEVRAPLVYWWLSETPKRQTSSLFYQFCGSLEVLFQ
proteinHuman alphaherpesvirus 1 strain KOSA0A110B4Q71–296monomerMolecule count 133.907 kDa
Tegument protein UL51
View sequence
MASLLGAISGWGARPEEQYEMIRAAVPPSEAEPRLQEALVVVNALLPAPITLDDALGSLDDTRRLVKARALARTYHACMVNLERLARHHPGLEAPTIDGAVAAHQDKMRRLADTCMATILQMYMSVGAADKSADVLVSQAIRSMAESDVVMEDVAIAERALGLSAFGVAGGTRSGGLGVTEAPSLGHPHTPPPEVTLAPAARNGDALPDPKPESCPRVSVPRPTASPTAPRPGPSRAAPCVLGQ
proteinHuman alphaherpesvirus 1D3YPL01–244dimerMolecule count 225.448 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
12632[3]0.0224526–7.31483 1/nmHas uncertainty columnMissing 056sasbdb/entries/57/sasdg57/source/SASDG57.dat
▼

2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)18.22—nm
i0Guinier4538.449.56arbitrary
i0P(r)4643.0—arbitrary
mwExperimental84.0—kDa
mwPorod100.0—kDa
porod_volumePorod160.0—nm³
rgGuinier3.950.07nm
rgP(r)4.296—nm

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

Fit 1 · GASBOR

χ²: 1.08CorMap p: 0.131158Unit: 1/A

Monomer component fit, 80% volume fraction

ModelName / TypeSoftwareSymmetryModel MWPDB DeclarationSource file
1—dummyGASBOR ———Model Image

Fit 2 · GASBOR GASBORMX

χ²: 1.0CorMap p: 0.363345Unit: 1/A

Dimer component fit, 20% volume fraction

ModelName / TypeSoftwareSymmetryModel MWPDB DeclarationSource file
1—dummyGASBOR P2——Model Image
▶

4. Source File Index Source Files

▶

5. Experiment Description and Publication Experiment & Publication

▼

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 time0.995Frames35
Wavelength0.124Sample-to-detector distance3.0
SourceX-ray synchrotronDetectorPilatus 6M
Facility / beamlinePETRA III / EMBL P12 · DESY; Hamburg, Germany
q range0.022 – 7.315Sample 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
codeSASDG57
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/SASDG57.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDG57.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDG57_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDG57_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDG57_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDG57_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDG57.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].oligomerizationmonomer
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_mw33.907
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_nameTegument protein UL51
experiment.sample.molecule[1].short_namepUL51
experiment.sample.molecule[1].sequenceMASLLGAISGWGARPEEQYEMIRAAVPPSEAEPRLQEALVVVNALLPAPITLDDALGSLDDTRRLVKARALARTYHACMVNLERLARHHPGLEAPTIDGAVAAHQDKMRRLADTCMATILQMYMSVGAADKSADVLVSQAIRSMAESDVVMEDVAIAERALGLSAFGVAGGTRSGGLGVTEAPSLGHPHTPPPEVTLAPAARNGDALPDPKPESCPRVSVPRPTASPTAPRPGPSRAAPCVLGQ
experiment.sample.molecule[1].organismHuman alphaherpesvirus 1
experiment.sample.molecule[1].uniprot_codeD3YPL0
experiment.sample.molecule[1].uniprot_range_first1
experiment.sample.molecule[1].uniprot_range_last244
experiment.sample.molecule[1].oligomerizationdimer
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_mw50.896
experiment.sample.molecule[1].number_molecules2
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.name1:2 heterotrimer 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_frames35
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_max7.315
experiment.total_exposure_timenull
experiment.seccolumn1
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fits[0].models[0].symmetrynull
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fits[0].models[0].user502
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fits[0].chi_square_value1.08
fits[0].p_value0.131158
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fits[1].chi_square_value1.0
fits[1].p_value0.363345
fits[1].fit_residual_plotSASDG57_fit2_fitresiduals_img.png
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fits[1].fit_lognull
fits[1].software_versionGASBORMX
fits[1].descriptionDimer component fit, 20% volume fraction
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionThe quoted experimental molecular mass, that corresponds to a 1:2 pUL7:pUL51 heterotrimer, was determined from SEC-MALLS-RI measurements performed in parallel to the SEC-SAXS. The SEC-SAXS data, Rg correlations through the heterotrimer 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 an 80 % volume fraction of the heterotrimer (corresponding fit, top) combined with a 20% volume fraction of a 2:4 pUL7:pUL51 heterohexamer (corresponding fit, bottom), due to incomplete SEC-separation between the two forms of the complex (also refer to SASBDB entry SASDG47).
experiment_descriptionSynchrotron SAXS data from the 1:2 heterotrimer 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. 35 successive 0.995 second frames were collected through the major 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_mw84.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw100.0
porod_mw_errornull
pddf_i04643.0
pddf_i0_errornull
guinier_i04538.44
guinier_i0_error9.56
pddf_rg4.296
pddf_rg_errornull
guinier_rg3.95
guinier_rg_error0.07
pddf_dmax18.22
pddf_dmax_errornull
porod_volume160.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first39
guinier_point_last108
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDG57_datloglog_img.png
symmetrynull
last_modified2023-06-21T07:55:24.740692+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDG57
statussuccess
started_at2026-08-11T15:22:19.403265+00:00
finished_at2026-08-11T15:22:40.491870+00:00
source_last_modified2023-06-21T07:55:24.740692+02:00
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View the complete summary.json source
{
  "code": "SASDG57",
  "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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        "resolution": null
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      "name": "PETRA III",
      "city": "DESY; Hamburg",
      "country": "Germany",
      "beamline_name": "EMBL P12",
      "beam_geometry": null,
      "type_of_source": "X-ray synchrotron",
      "point_source": null,
      "line_collimation": null,
      "sample_path_length": null,
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          "long_name": "Tegument protein UL7",
          "short_name": "pUL7",
          "sequence": "MAAATADDEGSAATILKQAIAGDRSLVEAAEAISQQTLLRLACEVRQVGDRQPRFTATSIARVDVAPGCRLRFVLDGSPEDAYVTSEDYFKRCCGQSSYRGFAVAVLTANEDHVHSLAVPPLVLLHRFSLFNPRDLLDFELACLLMYLENCPRSHATPSTFAKVLAWLGVAGRRTSPFERVRCLFLRSCHWVLNTLMFMVHVKPFDDEFVLPHWYMARYLLANNPPPVLSALFCATPTSSSFRLPGPPPRSDCVAYNPAGIMGSCWASEEVRAPLVYWWLSETPKRQTSSLFYQFCGSLEVLFQ",
          "organism": "Human alphaherpesvirus 1 strain KOS",
          "uniprot_code": "A0A110B4Q7",
          "uniprot_range_first": 1,
          "uniprot_range_last": 296,
          "oligomerization": "monomer",
          "molecular_type": "protein",
          "uniprot_sequence": "MAAATADDEGSAATILKQAIAGDRSLVEAAEAISQQTLLRLACEVRQVGDRQPRFTATSI\nARVDVAPGCRLRFVLDGSPEDAYVTSEDYFKRCCGQSSYRGFAVAVLTANEDHVHSLAVP\nPLVLLHRFSLFNPRDLLDFELACLLMYLENCPRSHATPSTFAKVLAWLGVAGRRTSPFER\nVRCLFLRSCHWVLNTLMFMVHVKPFDDEFVLPHWYMARYLLANNPPPVLSALFCATPTSS\nSFRLPGPPPRSDCVAYNPAGIMGSCWASEEVRAPLVYWWLSETPKRQTSSLFYQFC",
          "mw": 33.907,
          "total_mw": 33.907,
          "number_molecules": 1,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        },
        {
          "long_name": "Tegument protein UL51",
          "short_name": "pUL51",
          "sequence": "MASLLGAISGWGARPEEQYEMIRAAVPPSEAEPRLQEALVVVNALLPAPITLDDALGSLDDTRRLVKARALARTYHACMVNLERLARHHPGLEAPTIDGAVAAHQDKMRRLADTCMATILQMYMSVGAADKSADVLVSQAIRSMAESDVVMEDVAIAERALGLSAFGVAGGTRSGGLGVTEAPSLGHPHTPPPEVTLAPAARNGDALPDPKPESCPRVSVPRPTASPTAPRPGPSRAAPCVLGQ",
          "organism": "Human alphaherpesvirus 1",
          "uniprot_code": "D3YPL0",
          "uniprot_range_first": 1,
          "uniprot_range_last": 244,
          "oligomerization": "dimer",
          "molecular_type": "protein",
          "uniprot_sequence": "MASLLGAICGWGARPEEQYEMIRAAVPPSEAEPRLQEALVVVNALLPAPITLDDALGSLD\nDTRRLVKARALARTYHACMVNLERLARHHPGLEAPTIDGAVAAHQDKMRRLADTCMATIL\nQMYMSVGAADKSADVLVSQAIRSMAESDVVMEDVAIAERALGLSAFGVAGGTRSGGLGVT\nEAPSLGHPHTPPPEVTLAPAARNGDALPDPKPESCPRVSVPRPTASPTAPRPGPSRAAPC\nVLGQ",
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          "number_molecules": 2,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
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        "name": "20 mM HEPES, 200 mM NaCl, 3% (v/v) glycerol, 1 mM DTT",
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        "pka": null,
        "ph": 7.5,
        "deuteration": null
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      "purity_method": null,
      "name": "1:2 heterotrimer of pUL7 and pUL51 from herpes simplex virus 1",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
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    "contributor": [
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        "affiliation": [
          {
            "short_name": null,
            "address": null,
            "full_name": "University of Cambridge",
            "webpage": null
          }
        ],
        "contributor_name": "Benjamin",
        "contributor_surname": "Butt",
        "orcid": "https://orcid.org/0000-0001-6718-0470"
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    "concentration_method": null,
    "concentration_unit": null,
    "date": "2019-05-16",
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    "cell_temperature": 20.2,
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    "flow_rate": 0.5,
    "s_min": 0.022,
    "s_max": 7.315,
    "total_exposure_time": null,
    "seccolumn": 1
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      "chi_square_value": 1.08,
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  "description": "The quoted experimental molecular mass, that corresponds to a 1:2 pUL7:pUL51 heterotrimer, was determined from SEC-MALLS-RI measurements performed in parallel to the SEC-SAXS. The SEC-SAXS data, Rg correlations through the heterotrimer 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 an 80 % volume fraction of the heterotrimer (corresponding fit, top) combined with a 20% volume fraction of a 2:4 pUL7:pUL51 heterohexamer (corresponding fit, bottom), due to incomplete SEC-separation between the two forms of the complex (also refer to SASBDB entry SASDG47).",
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  "last_modified": "2023-06-21T07:55:24.740692+02:00",
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}
View the complete manifest.json source
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