SASDDD8

class II apurinic/apyrimidinic-endonuclease/3'-5' exonuclease III

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2020-08-13T15:34:48.952980+02:00

CAUTION! The SAXS data at very-low angles (s < 0.21 nm-1) have error estimates and intensities that are unrealistic for a single-concentration SAXS profile and are inconsistent with the remaining dataset.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · class II apurinic/apyrimidinic-endonuclease/3'-5' exonuclease III

Concentration— – 5.3 Buffer / pH50 mM Tris-HCl 500 mM NaCl 5mM β-mercaptoethanol / 8.0
Experimental temperature10.0 Facility / beamlineESRF / BM29
Wavelength0.082 nmExposure1.0 s × 10

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Probable exodeoxyribonuclease III protein XthA
View sequence
MPDGTIDGGHPQRPASPRLRSPLLRLATWNVNSIRTRLDRVLDWLGRADVDVLAMQETKCPDGQFPALPLFELGYDVAHVGFDQWNGVAIASRVGLDDVRVGFDGQPSWSGKPEVAATTEARALGATCGGIRVWSLYVPNGRALDDPHYTYKLDWLAALRDTAEGWLRDDPAAPIALMGDWNIAPTDDDVWSTEFFAGCTHVSEPERKAFNAIVDAQFTDVVRPFTPGPGVYTYWDYTQLRFPKKQGMRIDFILGSPALAARVMDAQIVREERKGKAPSDHAPVLVDLHAG
proteinMycobacterium tuberculosisA0A0T9L2511–291monomerMolecule count 132.108 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11037[3]0.03082862–4.944437 1/nmHas uncertainty columnMissing 010sasbdb/entries/d8/sasddd8/source/SASDDD8.dat
▼

2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)7.31—nm
i0Guinier13.630.013arbitrary
i0P(r)13.54—arbitrary
mwExperimental35.65—kDa
porod_volumePorod56.2—nm³
rgGuinier2.370.012nm
rgP(r)2.353—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

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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 name50 mM Tris-HCl 500 mM NaCl 5mM β-mercaptoethanolBuffer concentration—
pH8.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2017-05-12Storage / measurement temperature4.0 / 10.0
Exposure time1.0Frames10
Wavelength0.082Sample-to-detector distance1.1
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineESRF / BM29 · Grenoble, France
q range0.031 – 4.944Sample 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

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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:156 field values
Field pathRaw value
codeSASDDD8
statusPublished
type_of_curveSingle concentration
angular_unit1/nm
project.titleM. tuberculosis class II apurinic/ apyrimidinic-endonuclease/3'-5' exonuclease (XthA) engages with NAD+-dependent DNA ligase A (LigA) to counter futile cleavage and ligation cycles in base excision repair.
project.publication.titleM. tuberculosis class II apurinic/ apyrimidinic-endonuclease/3'-5' exonuclease (XthA) engages with NAD+-dependent DNA ligase A (LigA) to counter futile cleavage and ligation cycles in base excision repair.
project.publication.author_listKhanam T, Afsar M, Shukla A, Alam F, Kumar S, Soyar H, Dolma K, Pasupuleti M, Srivastava KK, Ampapathi RS, Ramachandran R
project.publication.journalNucleic Acids Res
project.publication.doi10.1093/nar/gkaa188
project.publication.pmid32232338
project.publication.published_date2020 Mar 30
project.statusreleased
project.submitted_date2018-09-06
project.released_date2019-05-28
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDDD8.out
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experiment.instrument.detector.typeDectris
experiment.instrument.detector.namePilatus 1M
experiment.instrument.detector.resolution172.0
experiment.instrument.nameESRF
experiment.instrument.cityGrenoble
experiment.instrument.countryFrance
experiment.instrument.beamline_nameBM29
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_nameProbable exodeoxyribonuclease III protein XthA
experiment.sample.molecule[0].short_nameMtbXthA
experiment.sample.molecule[0].sequenceMPDGTIDGGHPQRPASPRLRSPLLRLATWNVNSIRTRLDRVLDWLGRADVDVLAMQETKCPDGQFPALPLFELGYDVAHVGFDQWNGVAIASRVGLDDVRVGFDGQPSWSGKPEVAATTEARALGATCGGIRVWSLYVPNGRALDDPHYTYKLDWLAALRDTAEGWLRDDPAAPIALMGDWNIAPTDDDVWSTEFFAGCTHVSEPERKAFNAIVDAQFTDVVRPFTPGPGVYTYWDYTQLRFPKKQGMRIDFILGSPALAARVMDAQIVREERKGKAPSDHAPVLVDLHAG
experiment.sample.molecule[0].organismMycobacterium tuberculosis
experiment.sample.molecule[0].uniprot_codeA0A0T9L251
experiment.sample.molecule[0].uniprot_range_first1
experiment.sample.molecule[0].uniprot_range_last291
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequencenull
experiment.sample.molecule[0].mw32.108
experiment.sample.molecule[0].total_mw32.108
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.name50 mM Tris-HCl 500 mM NaCl 5mM β-mercaptoethanol
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.nameclass II apurinic/apyrimidinic-endonuclease/3'-5' exonuclease III
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].addressIndia
experiment.contributor[0].affiliation[0].full_nameCSIR - Central Drug Research Institute
experiment.contributor[0].affiliation[0].webpagehttps://cdri.res.in/
experiment.contributor[0].contributor_nameRavishankar
experiment.contributor[0].contributor_surnameRamachandran
experiment.contributor[0].orcid
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experiment.concentration_unitnull
experiment.date2017-05-12
experiment.storage_temperature4.0
experiment.cell_temperature10.0
experiment.exposure_time1.0
experiment.number_of_frames10
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pddf_software_version5.0
i0_calibration_standardnull
descriptionCAUTION! The SAXS data at very-low angles (s < 0.21 nm-1) have error estimates and intensities that are unrealistic for a single-concentration SAXS profile and are inconsistent with the remaining dataset.
experiment_descriptionSynchrotron SAXS data from solutions of the class II apurinic/apyrimidinic-endonuclease/3'-5' exonuclease III in 50 mM Tris-HCl 500 mM NaCl 5mM β-mercaptoethanol, pH 8 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 1.1 m and at a wavelength of λ = 0.082 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.30 mg/ml was measured at 10°C. 10 successive 1 second frames were collected. 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_mw35.65
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i013.54
pddf_i0_errornull
guinier_i013.63
guinier_i0_error0.013
pddf_rg2.353
pddf_rg_errornull
guinier_rg2.37
guinier_rg_error0.012
pddf_dmax7.31
pddf_dmax_errornull
porod_volume56.2
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first22
guinier_point_last110
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDDD8_datloglog_img.png
symmetrynull
last_modified2020-08-13T15:34:48.952980+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDDD8
statussuccess
started_at2026-08-11T16:27:40.378176+00:00
finished_at2026-08-11T16:27:52.378992+00:00
source_last_modified2020-08-13T15:34:48.952980+02:00
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View the complete summary.json source
{
  "code": "SASDDD8",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/nm",
  "project": {
    "title": "M. tuberculosis class II apurinic/ apyrimidinic-endonuclease/3'-5' exonuclease (XthA) engages with NAD+-dependent DNA ligase A (LigA) to counter futile cleavage and ligation cycles in base excision repair.",
    "publication": {
      "title": "M. tuberculosis class II apurinic/ apyrimidinic-endonuclease/3'-5' exonuclease (XthA) engages with NAD+-dependent DNA ligase A (LigA) to counter futile cleavage and ligation cycles in base excision repair.",
      "author_list": "Khanam T, Afsar M, Shukla A, Alam F, Kumar S, Soyar H, Dolma K, Pasupuleti M, Srivastava KK, Ampapathi RS, Ramachandran R",
      "journal": "Nucleic Acids Res",
      "doi": "10.1093/nar/gkaa188",
      "pmid": "32232338",
      "published_date": "2020 Mar 30"
    },
    "status": "released",
    "submitted_date": "2018-09-06",
    "released_date": "2019-05-28"
  },
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          "long_name": "Probable exodeoxyribonuclease III protein XthA",
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      "ext_coefficient": null,
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View the complete manifest.json source
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