SASDCX8

Human Rev7 monomer (R124A mutant) in complex with Rev3 peptide @ 6mg/mL

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2019-12-06T13:07:15.624532+01:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Human Rev7 monomer (R124A mutant) in complex with Rev3 peptide @ 6mg/mL

Concentration— – 6.0 Buffer / pH20 mM Tris, 150 mM NaCl, 1 mM EDTA, 10 mM DTT, 5% glycerol / 8.4
Experimental temperature4.0 Facility / beamlineCornell High Energy Synchrotron Source (CHESS) / G1
Wavelength0.1267 nmExposure1.0 s × 10

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Mitotic spindle assembly checkpoint protein MAD2B
View sequence
GMTTLTRQDLNFGQVVADVLCEFLEVAVHLILYVREVYPVGIFQKRKKYNVPVQMSCHPELNQYIQDTLHCVKPLLEKNDVEKVVVVILDKEHRPVEKFVFEITQPPLLSISSDSLLSHVEQLLAAFILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEKIQVIKDFPWILADEQDVHMHDPRLIPLKTMTSDILKMQLYVEERAHKGS
proteinHomo sapiensQ9UI951–211monomerMolecule count 124.306 kDa
DNA polymerase zeta catalytic subunit
View sequence
MEDKKIVIMPCKCAPSRQLVQVWLQAKE
proteinHomo sapiensO606731988–2014monomerMolecule count 13.273 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1742[3]0.008592058–0.8018937 1/AHas uncertainty columnMissing 00sasbdb/entries/x8/sasdcx8/source/SASDCX8.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)7.59—Å
i0Guinier0.1048.1e-05—
i0P(r)0.1040.00012—
mwExperimental26.9—kDa
mwGuinier I(0)26.90.02kDa
mwPorod27.4—kDa
porod_volumePorod46.6—ų
rgGuinier2.070.003Å
rgP(r)2.070.004Å

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, 150 mM NaCl, 1 mM EDTA, 10 mM DTT, 5% glycerolBuffer concentration—
pH8.4Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2016-05-14Storage / measurement temperature4.0 / 4.0
Exposure time1.0Frames10
Wavelength0.1267Sample-to-detector distance—
SourceX-ray synchrotronDetectorFinger Lakes CCD
Facility / beamlineCornell High Energy Synchrotron Source (CHESS) / G1 · Ithaca, NY, USA
q range0.086 – 8.019Sample 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

CategoryFileStatusSizeChecksumDownload and View
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full_entry_zip:source record and ZIP contents (4 items)
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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:176 field values
Field pathRaw value
codeSASDCX8
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleRev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex.
project.publication.titleRev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex.
project.publication.author_listRizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
project.publication.journalProc Natl Acad Sci U S A
project.publication.doi10.1073/pnas.1801149115
project.publication.pmid30111544
project.publication.published_date2018 Aug 28
project.statusreleased
project.submitted_date2017-11-14
project.released_date2018-07-31
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDCX8.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDCX8.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDCX8_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDCX8_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDCX8_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDCX8_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDCX8.sascif
experiment.instrument.detector.typeCCD
experiment.instrument.detector.nameFinger Lakes CCD
experiment.instrument.detector.resolution0.0
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_nameMitotic spindle assembly checkpoint protein MAD2B
experiment.sample.molecule[0].short_namehRev7-R124A
experiment.sample.molecule[0].sequenceGMTTLTRQDLNFGQVVADVLCEFLEVAVHLILYVREVYPVGIFQKRKKYNVPVQMSCHPEL NQYIQDTLHCVKPLLEKNDVEKVVVVILDKEHRPVEKFVFEITQPPLLSISSDSLLSHVE QLLAAFILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEKIQVIKDFPWILADEQDVH MHDPRLIPLKTMTSDILKMQLYVEERAHKGS
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeQ9UI95
experiment.sample.molecule[0].uniprot_range_first1
experiment.sample.molecule[0].uniprot_range_last211
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMTTLTRQDLNFGQVVADVLCEFLEVAVHLILYVREVYPVGIFQKRKKYNVPVQMSCHPEL NQYIQDTLHCVKPLLEKNDVEKVVVVILDKEHRPVEKFVFEITQPPLLSISSDSLLSHVE QLLRAFILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEKIQVIKDFPWILADEQDVH MHDPRLIPLKTMTSDILKMQLYVEERAHKGS
experiment.sample.molecule[0].mw24.306
experiment.sample.molecule[0].total_mw24.306
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_nameDNA polymerase zeta catalytic subunit
experiment.sample.molecule[1].short_nameRev3-RBM2
experiment.sample.molecule[1].sequenceMEDK KIVIMPCKCA PSRQLVQVWL QAKE
experiment.sample.molecule[1].organismHomo sapiens
experiment.sample.molecule[1].uniprot_codeO60673
experiment.sample.molecule[1].uniprot_range_first1988
experiment.sample.molecule[1].uniprot_range_last2014
experiment.sample.molecule[1].oligomerizationmonomer
experiment.sample.molecule[1].molecular_typeprotein
experiment.sample.molecule[1].uniprot_sequenceMFSVRIVTADYYMASPLQGLDTCQSPLTQAPVKKVPVVRVFGATPAGQKTCLHLHGIFPY LYVPYDGYGQQPESYLSQMAFSIDRALNVALGNPSSTAQHVFKVSLVSGMPFYGYHEKER HFMKIYLYNPTMVKRICELLQSGAIMNKFYQPHEAHIPYLLQLFIDYNLYGMNLINLAAV KFRKARRKSNTLHATGSCKNHLSGNSLADTLFRWEQDEIPSSLILEGVEPQSTCELEVDA VAADILNRLDIEAQIGGNPGLQAIWEDEKQRRRNRNETSQMSQPESQDHRFVPATESEKK FQKRLQEILKQNDFSVTLSGSVDYSDGSQEFSAELTLHSEVLSPEMLQCTPANMVEVHKD KESSKGHTRHKVEEALINEEAILNLMENSQTFQPLTQRLSESPVFMDSSPDEALVHLLAG LESDGYRGERNRMPSPCRSFGNNKYPQNSDDEENEPQIEKEEMELSLVMSQRWDSNIEEH CAKKRSLCRNTHRSSTEDDDSSSGEEMEWSDNSLLLASLSIPQLDGTADENSDNPLNNEN SRTHSSVIATSKLSVKPSIFHKDAATLEPSSSAKITFQCKHTSALSSHVLNKEDLIEDLS QTNKNTEKGLDNSVTSFTNESTYSMKYPGSLSSTVHSENSHKENSKKEILPVSSCESSIF DYEEDIPSVTRQVPSRKYTNIRKIEKDSPFIHMHRHPNENTLGKNSFNFSDLNHSKNKVS SEGNEKGNSTALSSLFPSSFTENCELLSCSGENRTMVHSLNSTADESGLNKLKIRYEEFQ EHKTEKPSLSQQAAHYMFFPSVVLSNCLTRPQKLSPVTYKLQPGNKPSRLKLNKRKLAGH QETSTKSSETGSTKDNFIQNNPCNSNPEKDNALASDLTKTTRGAFENKTPTDGFIDCHFG DGTLETEQSFGLYGNKYTLRAKRKVNYETEDSESSFVTHNSKISLPHPMEIGESLDGTLK SRKRRKMSKKLPPVIIKYIIINRFRGRKNMLVKLGKIDSKEKQVILTEEKMELYKKLAPL KDFWPKVPDSPATKYPIYPLTPKKSHRRKSKHKSAKKKTGKQQRTNNENIKRTLSFRKKR SHAILSPPSPSYNAETEDCDLNYSDVMSKLGFLSERSTSPINSSPPRCWSPTDPRAEEIM AAAEKEAMLFKGPNVYKKTVNSRIGKTSRARAQIKKSKAKLANPSIVTKKRNKRNQTNKL VDDGKKKPRAKQKTNEKGTSRKHTTLKDEKIKSQSGAEVKFVLKHQNVSEFASSSGGSQL LFKQKDMPLMGSAVDHPLSASLPTGINAQQKLSGCFSSFLESKKSVDLQTFPSSRDDLHP SVVCNSIGPGVSKINVQRPHNQSAMFTLKESTLIQKNIFDLSNHLSQVAQNTQISSGMSS KIEDNANNIQRNYLSSIGKLSEYRNSLESKLDQAYTPNFLHCKDSQQQIVCIAEQSKHSE TCSPGNTASEESQMPNNCFVTSLRSPIKQIAWEQKQRGFILDMSNFKPERVKPRSLSEAI SQTKALSQCKNRNVSTPSAFGEGQSGLAVLKELLQKRQQKAQNANTTQDPLSNKHQPNKN ISGSLEHNKANKRTRSVTSPRKPRTPRSTKQKEKIPKLLKVDSLNLQNSSQLDNSVSDDS PIFFSDPGFESCYSLEDSLSPEHNYNFDINTIGQTGFCSFYSGSQFVPADQNLPQKFLSD AVQDLFPGQAIEKNEFLSHDNQKCDEDKHHTTDSASWIRSGTLSPEIFEKSTIDSNENRR HNQWKNSFHPLTTRSNSIMDSFCVQQAEDCLSEKSRLNRSSVSKEVFLSLPQPNNSDWIQ GHTRKEMGQSLDSANTSFTAILSSPDGELVDVACEDLELYVSRNNDMLTPTPDSSPRSTS SPSQSKNGSFTPRTANILKPLMSPPSREEIMATLLDHDLSETIYQEPFCSNPSDVPEKPR EIGGRLLMVETRLANDLAEFEGDFSLEGLRLWKTAFSAMTQNPRPGSPLRSGQGVVNKGS SNSPKMVEDKKIVIMPCKCAPSRQLVQVWLQAKEEYERSKKLPKTKPTGVVKSAENFSSS VNPDDKPVVPPKMDVSPCILPTTAHTKEDVDNSQIALQAPTTGCSQTASESQMLPPVASA SDPEKDEDDDDNYYISYSSPDSPVIPPWQQPISPDSKALNGDDRPSSPVEELPSLAFENF LKPIKDGIQKSPCSEPQEPLVISPINTRARTGKCESLCFHSTPIIQRKLLERLPEAPGLS PLSTEPKTQKLSNKKGSNTDTLRRVLLTQAKNQFAAVNTPQKETSQIDGPSLNNTYGFKV SIQNLQEAKALHEIQNLTLISVELHARTRRDLEPDPEFDPICALFYCISSDTPLPDTEKT ELTGVIVIDKDKTVFSQDIRYQTPLLIRSGITGLEVTYAADEKALFHEIANIIKRYDPDI LLGYEIQMHSWGYLLQRAAALSIDLCRMISRVPDDKIENRFAAERDEYGSYTMSEINIVG RITLNLWRIMRNEVALTNYTFENVSFHVLHQRFPLFTFRVLSDWFDNKTDLYRWKMVDHY VSRVRGNLQMLEQLDLIGKTSEMARLFGIQFLHVLTRGSQYRVESMMLRIAKPMNYIPVT PSVQQRSQMRAPQCVPLIMEPESRFYSNSVLVLDFQSLYPSIVIAYNYCFSTCLGHVENL GKYDEFKFGCTSLRVPPDLLYQVRHDITVSPNGVAFVKPSVRKGVLPRMLEEILKTRFMV KQSMKAYKQDRALSRMLDARQLGLKLIANVTFGYTSANFSGRMPCIEVGDSIVHKARETL ERAIKLVNDTKKWGARVVYGDTDSMFVLLKGATKEQSFKIGQEIAEAVTATNPKPVKLKF EKVYLPCVLQTKKRYVGYMYETLDQKDPVFDAKGIETVRRDSCPAVSKILERSLKLLFET RDISLIKQYVQRQCMKLLEGKASIQDFIFAKEYRGSFSYKPGACVPALELTRKMLTYDRR SEPQVGERVPYVIIYGTPGVPLIQLVRRPVEVLQDPTLRLNATYYITKQILPPLARIFSL IGIDVFSWYHELPRIHKATSSSRSEPEGRKGTISQYFTTLHCPVCDDLTQHGICSKCRSQ PQHVAVILNQEIRELERQQEQLVKICKNCTGCFDRHIPCVSLNCPVLFKLSRVNRELSKA PYLRQLLDQF
experiment.sample.molecule[1].mw3.273
experiment.sample.molecule[1].total_mw3.273
experiment.sample.molecule[1].number_molecules1
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 Tris, 150 mM NaCl, 1 mM EDTA, 10 mM DTT, 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.ph8.4
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameHuman Rev7 monomer (R124A mutant) in complex with Rev3 peptide @ 6mg/mL
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].addressStorrs, CT, USA
experiment.contributor[0].affiliation[0].full_nameUniversity of Connecticut
experiment.contributor[0].affiliation[0].webpagehttps://uconn.edu/
experiment.contributor[0].contributor_nameAlex
experiment.contributor[0].contributor_surnameRizzo
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2016-05-14
experiment.storage_temperature4.0
experiment.cell_temperature4.0
experiment.exposure_time1.0
experiment.number_of_frames10
experiment.wavelength0.1267
experiment.sample_detector_distancenull
experiment.concentration_minnull
experiment.concentration_max6.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.086
experiment.s_max8.019
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].softwarePDB (Protein Data Bank)
fits[0].models[0].pdb_link[0].pdb_code6bc8
fits[0].models[0].pdb_link[0].ext_code6BC8
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fits[0].models[0].model_titlenull
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fits[0].models[0].model_mw27.54
fits[0].models[0].bead_radius1.9
fits[0].models[0].lognull
fits[0].models[0].symmetry
fits[0].models[0].commentresidues at N- and C-termini that were missing in PDB were built in extended conformation
fits[0].models[0].user249
fits[0].fit_unit1/A
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fits[0].softwareFoXS
fits[0].chi_square_value5.694771
fits[0].p_value0.0
fits[0].fit_residual_plotSASDCX8_fit1_fitfoxsresiduals_img.png
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fits[0].fit_lognull
fits[0].software_version
fits[0].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionATSAS GNOM
i0_calibration_standardnull
descriptionnull
experiment_descriptionnull
tags[]
intensity_unitnull
experimental_mw26.9
experimental_mw_errornull
guinier_i0_mw26.9
guinier_i0_mw_error0.02
porod_mw27.4
porod_mw_errornull
pddf_i00.104
pddf_i0_error0.00012
guinier_i00.104
guinier_i0_error8.1e-05
pddf_rg2.07
pddf_rg_error0.004
guinier_rg2.07
guinier_rg_error0.003
pddf_dmax7.59
pddf_dmax_errornull
porod_volume46.6
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first1
guinier_point_last95
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDCX8_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDCX8
statussuccess
started_at2026-08-11T16:02:43.374725+00:00
finished_at2026-08-11T16:02:52.562083+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDCX8",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex.",
    "publication": {
      "title": "Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex.",
      "author_list": "Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM",
      "journal": "Proc Natl Acad Sci U S A",
      "doi": "10.1073/pnas.1801149115",
      "pmid": "30111544",
      "published_date": "2018 Aug 28"
    },
    "status": "released",
    "submitted_date": "2017-11-14",
    "released_date": "2018-07-31"
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View the complete manifest.json source
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