SASDDQ9

N-terminal half of herpes simplex virus type-1 inner tegument protein UL37

Data type: SASBDB experimental data Status: Published Curve type: SEC-SAS Last updated: 2019-12-06T13:07:15.624532+01:00

Additional SEC parameters: Column type: Superdex 200 Increase 5/150 GE; Flow rate: 0.3 mL/min; Sample injection concentration: 6 mg/ml; Injection volume: 100 µl.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · N-terminal half of herpes simplex virus type-1 inner tegument protein UL37

Concentration— – 6.0 Buffer / pH100 mM HEPES 150 mM NaCl 5% glycerol 0.1 mM tris(2-carboxyethyl)phosphine (TCEP) / 7.5
Experimental temperature4.0 Facility / beamlineCornell High Energy Synchrotron Source (CHESS) / G1
Wavelength0.124662 nmExposure2.0 s × 300

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Inner tegument protein
View sequence
GPGSMADRGPPSEAPVVTTSPAGPPSDGPMQRLLASLAGLRQPPTPTAETANGADDPAFLATAKLRAAMAAFLLSGTAIAPADARDCWRPLLEHLCALHRAHGLPETALLAENLPGLLVHRLVVALPEAPDQAFREMEVIKDTILAVTGSDTSHALDSAGLRTAAALGPVRVRQCAVEWIDRWQTVTKSCLAMSPRTSIEALGETSLKMAPVPLGQPSANLTTPAYSLLFPAPFVQEGLRFLALVSNRVTLFSAHLQRIDDATLTPLTRALFTLALVDEYLTTPERGAVVPPPLLAQFQHTVREIDPAIMIPPLEANKMVRSREEVRVSTALSRVSPRSACAPPGTLMARVRTDVAVFDPDVPFLSSSALAVFQPAVSSLLQLGEQPSAGAQQRLLALLQQTWTLIQNTNSPSVVINTLIDAGFTPSHCTHYLSALEGFLAAGVPARTPTGHGLGEVQQLFGCIALAGSNVFGLAREYGYYANYVKTFRRVQGASEHTHGRLCEAVGLSGGVLSQTLARIMGPAVPTEHLASLRRALVGEFETAERRFSSGQPSLLRETALIWIDVYGQTHWDITPTTP
proteinHuman alphaherpesvirus 1P10221—–—monomerMolecule count 161.724 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1481[3]0.0074119959–0.280759 1/AHas uncertainty columnMissing 013sasbdb/entries/q9/sasddq9/source/SASDDQ9.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)10.4—Å
i0Guinier0.027868e-051/cm
i0P(r)0.02785—1/cm
mwExperimental63.0—kDa
porod_volumePorod91.0—ų
rgGuinier3.3341.4Å
rgP(r)3.38—Å

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

χ²: 1.145CorMap p: 0.108692Unit: 1/A
ModelName / TypeSoftwareSymmetryModel MWPDB DeclarationSource file
1—dummyDAMFILT 5.0P1, none60.98—Model Image
2—dummyDAMMIN P1, none60.575—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 name100 mM HEPES 150 mM NaCl 5% glycerol 0.1 mM tris(2-carboxyethyl)phosphine (TCEP)Buffer concentration—
pH7.5Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2017-06-03Storage / measurement temperature4.0 / 4.0
Exposure time2.0Frames300
Wavelength0.124662Sample-to-detector distance1.53109
SourceX-ray synchrotronDetectorPilatus 200K
Facility / beamlineCornell High Energy Synchrotron Source (CHESS) / G1 · Ithaca, NY, USA
q range0.074 – 2.808Sample 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

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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:169 field values
Field pathRaw value
codeSASDDQ9
statusPublished
type_of_curveSEC-SAS
angular_unit1/A
project.titleThe dynamic nature of the conserved tegument protein UL37 of herpesviruses.
project.publication.titleThe dynamic nature of the conserved tegument protein UL37 of herpesviruses.
project.publication.author_listKoenigsberg AL, Heldwein EE
project.publication.journalJ Biol Chem
project.publication.doi10.1074/jbc.RA118.004481
project.publication.pmid30166339
project.publication.published_date2018 Oct 12
project.statusreleased
project.submitted_date2018-07-16
project.released_date2018-09-07
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sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDDQ9.sascif
experiment.instrument.detector.typePilatus
experiment.instrument.detector.namePilatus 200K
experiment.instrument.detector.resolution172.0
experiment.instrument.nameCornell High Energy Synchrotron Source (CHESS)
experiment.instrument.cityIthaca, NY
experiment.instrument.countryUSA
experiment.instrument.beamline_nameG1
experiment.instrument.beam_geometry
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_nameInner tegument protein
experiment.sample.molecule[0].short_nameHSV1 UL37
experiment.sample.molecule[0].sequenceGPGSMADRGPPSEAPVVTTSPAGPPSDGPMQRLLASLAGLRQPPTPTAETANGADDPAFLATAKLRAAMAAFLLSGTAIAPADARDCWRPLLEHLCALHRAHGLPETALLAENLPGLLVHRLVVALPEAPDQAFREMEVIKDTILAVTGSDTSHALDSAGLRTAAALGPVRVRQCAVEWIDRWQTVTKSCLAMSPRTSIEALGETSLKMAPVPLGQPSANLTTPAYSLLFPAPFVQEGLRFLALVSNRVTLFSAHLQRIDDATLTPLTRALFTLALVDEYLTTPERGAVVPPPLLAQFQHTVREIDPAIMIPPLEANKMVRSREEVRVSTALSRVSPRSACAPPGTLMARVRTDVAVFDPDVPFLSSSALAVFQPAVSSLLQLGEQPSAGAQQRLLALLQQTWTLIQNTNSPSVVINTLIDAGFTPSHCTHYLSALEGFLAAGVPARTPTGHGLGEVQQLFGCIALAGSNVFGLAREYGYYANYVKTFRRVQGASEHTHGRLCEAVGLSGGVLSQTLARIMGPAVPTEHLASLRRALVGEFETAERRFSSGQPSLLRETALIWIDVYGQTHWDITPTTP
experiment.sample.molecule[0].organismHuman alphaherpesvirus 1
experiment.sample.molecule[0].uniprot_codeP10221
experiment.sample.molecule[0].uniprot_range_firstnull
experiment.sample.molecule[0].uniprot_range_lastnull
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMADRGLPSEAPVVTTSPAGPPSDGPMQRLLASLAGLRQPPTPTAETANGADDPAFLATAK LRAAMAAFLLSGTAIAPADARDCWRPLLEHLCALHRAHGLPETALLAENLPGLLVHRLVV ALPEAPDQAFREMEVIKDTILAVTGSDTSHALDSAGLRTAAALGPVRVRQCAVEWIDRWQ TVTKSCLAMSPRTSIEALGETSLKMAPVPLGQPSANLTTPAYSLLFPAPFVQEGLRFLAL VSNRVTLFSAHLQRIDDATLTPLTRALFTLALVDEYLTTPERGAVVPPPLLAQFQHTVRE IDPAIMIPPLEANKMVRSREEVRVSTALSRVSPRSACAPPGTLMARVRTDVAVFDPDVPF LSSSALAVFQPAVSSLLQLGEQPSAGAQQRLLALLQQTWTLIQNTNSPSVVINTLIDAGF TPSHCTHYLSALEGFLAAGVPARTPTGHGLGEVQQLFGCIALAGSNVFGLAREYGYYANY VKTFRRVQGASEHTHGRLCEAVGLSGGVLSQTLARIMGPAVPTEHLASLRRALVGEFETA ERRFSSGQPSLLRETALIWIDVYGQTHWDITPTTPATPLSALLPVGQPSHAPSVHLAAAT QIRFPALEGIHPNVLADPGFVPYVLALVVGDALRATCSAAYLPRPVEFALRVLAWARDFG LGYLPTVEGHRTKLGALITLLEPAARGGLGPTMQMADNIEQLLRELYVISRGAVEQLRPL VQLQPPPPPEVGTSLLLISMYALAARGVLQDLAERADPLIRQLEDAIVLLRLHMRTLSAF FECRFESDGRRLYAVVGDTPDRLGPWPPEAMGDAVSQYCSMYHDAKRALVASLASLRSVI TETTAHLGVCDELAAQVSHEDNVLAVVRREIHGFLSVVSGIHARASKLLSGDQVPGFCFM GQFLARWRRLSACYQAARAAAGPEPVAEFVQELHDTWKGLQTERAVVVAPLVSSADQRAA AIREVMAHAPEDAPPQSPAADRVVLTSRRDLGAWGDYSLGPLGQTTAVPDSVDLSRQGLA VTLSMDWLLMNELLRVTDGVFRASAFRPLAGPESPRDLEVRDAGNSLPAPMPMDAQKPEA YGHGPRQADREGAPHSNTPVEDDEMIPEDTVAPPTDLPLTSYQ
experiment.sample.molecule[0].mw61.724
experiment.sample.molecule[0].total_mw61.724
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.buffer.name100 mM HEPES 150 mM NaCl 5% glycerol 0.1 mM tris(2-carboxyethyl)phosphine (TCEP)
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.nameN-terminal half of herpes simplex virus type-1 inner tegument protein UL37
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].addressSomerville, MA, USA
experiment.contributor[0].affiliation[0].full_nameTufts University School of Medicine
experiment.contributor[0].affiliation[0].webpagehttps://www.tufts.edu/
experiment.contributor[0].contributor_nameAndrea
experiment.contributor[0].contributor_surnameKoenigsberg
experiment.contributor[0].orcid
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2017-06-03
experiment.storage_temperature4.0
experiment.cell_temperature4.0
experiment.exposure_time2.0
experiment.number_of_frames300
experiment.wavelength0.124662
experiment.sample_detector_distance1.53109
experiment.concentration_minnull
experiment.concentration_max6.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.074
experiment.s_max2.808
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].bead_radius2.75
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fits[0].models[1].commentnull
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fits[0].softwareDAMMIN
fits[0].chi_square_value1.145
fits[0].p_value0.108692
fits[0].fit_residual_plotSASDDQ9_fit1_fitresiduals_img.png
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fits[0].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionAdditional SEC parameters: Column type: Superdex 200 Increase 5/150 GE; Flow rate: 0.3 mL/min; Sample injection concentration: 6 mg/ml; Injection volume: 100 µl.
experiment_descriptionSynchrotron SAXS data, I(s) vs s (where s = 4πsinθ/λ, and 2θ is the scattering angle), were measured from the N-terminal half of herpes simplex virus type-1 inner tegument protein UL37 using continuous-flow size-exclusion chromatography SAXS (SEC-SAXS) on the G1 beam line at the Cornell High Energy Synchrotron Source (CHESS; Ithaca, NY, USA). Data were collected a using a Pilatus 200K detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.125 nm. The SEC mobile phase consisted of 100 mM HEPES, 150 mM NaCl, 5% glycerol ,0.1 mM tris(2-carboxyethyl)phosphine (TCEP), pH 7.5, (4°C). The SAXS data measured from the SEC-elution (sample peak and buffer; 300 successive 2 s frames) were normalized to the intensity of the transmitted beam and radially averaged. The scattering of an appropriate solvent-blank was subtracted from the sample frames to produce the scaled and averaged data displayed in this entry.
tags[]
intensity_unit1/cm
experimental_mw63.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i00.02785
pddf_i0_errornull
guinier_i00.02786
guinier_i0_error8e-05
pddf_rg3.38
pddf_rg_errornull
guinier_rg3.334
guinier_rg_error1.4
pddf_dmax10.4
pddf_dmax_errornull
porod_volume91.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first3
guinier_point_last55
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDDQ9_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDDQ9
statussuccess
started_at2026-08-11T16:29:02.382943+00:00
finished_at2026-08-11T16:29:10.870474+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDDQ9",
  "status": "Published",
  "type_of_curve": "SEC-SAS",
  "angular_unit": "1/A",
  "project": {
    "title": "The dynamic nature of the conserved tegument protein UL37 of herpesviruses.",
    "publication": {
      "title": "The dynamic nature of the conserved tegument protein UL37 of herpesviruses.",
      "author_list": "Koenigsberg AL, Heldwein EE",
      "journal": "J Biol Chem",
      "doi": "10.1074/jbc.RA118.004481",
      "pmid": "30166339",
      "published_date": "2018 Oct 12"
    },
    "status": "released",
    "submitted_date": "2018-07-16",
    "released_date": "2018-09-07"
  },
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          "uniprot_code": "P10221",
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            "address": "Somerville, MA, USA",
            "full_name": "Tufts University School of Medicine",
            "webpage": "https://www.tufts.edu/"
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        "contributor_name": "Andrea",
        "contributor_surname": "Koenigsberg",
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    "date": "2017-06-03",
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  "experiment_description": "Synchrotron SAXS data, I(s) vs s (where s = 4πsinθ/λ, and 2θ is the scattering angle), were measured from the N-terminal half of herpes simplex virus type-1 inner tegument protein UL37 using continuous-flow size-exclusion chromatography SAXS (SEC-SAXS) on the G1 beam line at the Cornell High Energy Synchrotron Source (CHESS; Ithaca, NY, USA). Data were collected a using a Pilatus 200K detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.125 nm. The SEC mobile phase consisted of 100 mM HEPES, 150 mM NaCl, 5% glycerol ,0.1 mM tris(2-carboxyethyl)phosphine (TCEP), pH 7.5, (4°C). The SAXS data measured from the SEC-elution (sample peak and buffer; 300 successive 2 s frames) were normalized to the intensity of the transmitted beam and radially averaged. The scattering of an appropriate solvent-blank was subtracted from the sample frames to produce the scaled and averaged data displayed in this entry.",
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  "symmetry": null,
  "last_modified": "2019-12-06T13:07:15.624532+01:00",
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}
View the complete manifest.json source
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