SASDBK6

Truncated construct of human p23 (1-131)

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

Samples were measured at 1 mg/mL and 2 mg/mL in 1 mm path-length mica cells. All curves were inspected for X-ray damage and aggregation. The experimental molecular weight was determined by analytical ultracentrifugation.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Truncated construct of human p23 (1-131)

Concentration1.0 – 2.0 Buffer / pH25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol / 7.5
Experimental temperature20.0 Facility / beamlineBrazilian Synchrotron Light Laboratory / SAXS1 Beamline
Wavelength0.1488 nmExposure30.0 s × 2

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Prostaglandin E synthase 3 (1-131)
View sequence
GSMQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMNNMG
proteinHomo sapiensQ151851–131monomerMolecule count 115.693 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1451[2]0.01076235–0.36850529 1/ANo uncertainty columnMissing 4510sasbdb/entries/k6/sasdbk6/source/SASDBK6.dat
▼

2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)7.0—Å
i0Guinier0.01633e-05—
i0P(r)0.016322e-05—
mwExperimental18.0—kDa
porod_volumePorod31.0—ų
rgGuinier1.910.06Å
rgP(r)1.9330.005Å

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

This entry has no source fit record.

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4. Source File Index Source Files

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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 name25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanolBuffer concentration—
pH7.5Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2013-06-21Storage / measurement temperature4.0 / 20.0
Exposure time30.0Frames2
Wavelength0.1488Sample-to-detector distance1.0
SourceX-ray synchrotronDetectorPilatus 300K
Facility / beamlineBrazilian Synchrotron Light Laboratory / SAXS1 Beamline · Campinas, Brazil
q range0.108 – 3.685Sample 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:134 field values
Field pathRaw value
codeSASDBK6
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleThe C-terminal region of the human p23 chaperone modulates its structure and function.
project.publication.titleThe C-terminal region of the human p23 chaperone modulates its structure and function.
project.publication.author_listSeraphim TV, Gava LM, Mokry DZ, Cagliari TC, Barbosa LR, Ramos CH, Borges JC
project.publication.journalArch Biochem Biophys
project.publication.doi10.1016/j.abb.2014.10.015
project.publication.pmid25447839
project.publication.published_date2015 Jan 1
project.statusreleased
project.submitted_date2016-09-13
project.released_date2016-10-05
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experiment.instrument.detector.type20Hz
experiment.instrument.detector.namePilatus 300K
experiment.instrument.detector.resolutionnull
experiment.instrument.nameBrazilian Synchrotron Light Laboratory
experiment.instrument.cityCampinas
experiment.instrument.countryBrazil
experiment.instrument.beamline_nameSAXS1 Beamline
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_nameProstaglandin E synthase 3 (1-131)
experiment.sample.molecule[0].short_namePTGES, Sba1, p23
experiment.sample.molecule[0].sequenceGSMQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRK GESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMNNMG
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeQ15185
experiment.sample.molecule[0].uniprot_range_first1
experiment.sample.molecule[0].uniprot_range_last131
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCID PNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNF DRFSEMMNNMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE
experiment.sample.molecule[0].mw15.693
experiment.sample.molecule[0].total_mw15.693
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.name25 mM Tris-HCl, 100 mM NaCl, 5 mM B-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.ph7.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameTruncated construct of human p23 (1-131)
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].addressSão Carlos - SP - Brasil
experiment.contributor[0].affiliation[0].full_nameInstituto de Química de São Carlos
experiment.contributor[0].affiliation[0].webpage
experiment.contributor[0].contributor_nameJúlio
experiment.contributor[0].contributor_surnameBorges
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2013-06-21
experiment.storage_temperature4.0
experiment.cell_temperature20.0
experiment.exposure_time30.0
experiment.number_of_frames2
experiment.wavelength0.1488
experiment.sample_detector_distance1.0
experiment.concentration_min1.0
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experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.108
experiment.s_max3.685
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionGNOM v4.5a
i0_calibration_standardnull
descriptionSamples were measured at 1 mg/mL and 2 mg/mL in 1 mm path-length mica cells. All curves were inspected for X-ray damage and aggregation. The experimental molecular weight was determined by analytical ultracentrifugation.
experiment_descriptionSynchrotron SAXS data from solutions of truncated human p23 (1-131) in 25 mM Tris-HCl, 100 mM NaCl, 5 mM β-mercaptoethanol, pH 7.5 were collected on the SAXS1 Beamline at the Brazilian Synchrotron Light Laboratory (Campinas, Brazil) using a 20Hz Pilatus 300K detector at a sample-detector distance of 1 m and at a wavelength of λ = 0.1488 nm (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle). Solute concentrations ranging between 1 and 2 mg/ml were measured at 20°C. Two successive 30 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_unitnull
experimental_mw18.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i00.01632
pddf_i0_error2e-05
guinier_i00.0163
guinier_i0_error3e-05
pddf_rg1.933
pddf_rg_error0.005
guinier_rg1.91
guinier_rg_error0.06
pddf_dmax7.0
pddf_dmax_errornull
porod_volume31.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first1
guinier_point_last71
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDBK6_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDBK6
statussuccess
started_at2026-08-11T16:40:41.695251+00:00
finished_at2026-08-11T16:40:49.379462+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDBK6",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "The C-terminal region of the human p23 chaperone modulates its structure and function.",
    "publication": {
      "title": "The C-terminal region of the human p23 chaperone modulates its structure and function.",
      "author_list": "Seraphim TV, Gava LM, Mokry DZ, Cagliari TC, Barbosa LR, Ramos CH, Borges JC",
      "journal": "Arch Biochem Biophys",
      "doi": "10.1016/j.abb.2014.10.015",
      "pmid": "25447839",
      "published_date": "2015 Jan 1"
    },
    "status": "released",
    "submitted_date": "2016-09-13",
    "released_date": "2016-10-05"
  },
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          "long_name": "Prostaglandin E synthase 3 (1-131)",
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View the complete manifest.json source
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