SASDDC6

Small glutamine-rich tetratricopeptide repeat-containing protein alpha (N-terminal-TPR domains; SGTA_NT)

Data type: SASBDB experimental data Status: Published Curve type: Merged Last updated: 2023-06-21T07:56:39.492710+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Small glutamine-rich tetratricopeptide repeat-containing protein alpha (N-terminal-TPR domains; SGTA_NT)

Concentration0.6 – 4.5 Buffer / pH10 mM potassium phosphate, 100 mM NaCl / 6.0
Experimental temperature25.0 Facility / beamlinePETRA III / EMBL P12
Wavelength0.124 nmExposure0.045 s × 20

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Small glutamine-rich tetratricopeptide repeat-containing protein alpha Nterminal-TPR domains
View sequence
GSMDNKKRLAYAIIQFLHDQLRHGGLSSDAQESLEVAIQCLETAFGVTVEDSDLALPQTLPEIFEAAATGKEMPQDLRSPARTPPSEEDSAEAERLKTEGNEQMKVENFEAAVHFYGKAIELNPANAVYFCNRAAAYSKLGNYAGAVQDCERAICIDPAYSKAYGRMGLALSSLNKHVEAVAYYKKALELDPDNETYKSNLKIAELKLREAPSPT
proteinHomo sapiensO437651–213dimerMolecule count 223.592 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11808[3]0.0269502–4.80121 1/nmHas uncertainty columnMissing 022sasbdb/entries/c6/sasddc6/source/SASDDC6.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
i0Guinier10844.016.0—
mwExperimental41.0—kDa
rgGuinier3.60.1nm

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

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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 name10 mM potassium phosphate, 100 mM NaClBuffer concentration—
pH6.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2015-06-05Storage / measurement temperature— / 25.0
Exposure time0.045Frames20
Wavelength0.124Sample-to-detector distance3.0
SourceX-ray synchrotronDetectorPilatus 2M
Facility / beamlinePETRA III / EMBL P12 · DESY; Hamburg, Germany
q range0.027 – 4.801Sample 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

Downloadable Files

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full_entry_zip:source record and ZIP contents (1 items)
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pddf:source record
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sascif:source record
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summary:source record
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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
codeSASDDC6
statusPublished
type_of_curveMerged
angular_unit1/nm
project.titleStructural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control.
project.publication.titleStructural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control.
project.publication.author_listMartínez-Lumbreras S, Krysztofinska EM, Thapaliya A, Spilotros A, Matak-Vinkovic D, Salvadori E, Roboti P, Nyathi Y, Muench JH, Roessler MM, Svergun DI, High S, Isaacson RL
project.publication.journalBMC Biol
project.publication.doi10.1186/s12915-018-0542-3
project.publication.pmid29996828
project.publication.published_date2018 Jul 11
project.statusreleased
project.submitted_date2018-05-02
project.released_date2018-06-11
pddf_datanull
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pddf_plotnull
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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
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experiment.sample.molecule[0].long_nameSmall glutamine-rich tetratricopeptide repeat-containing protein alpha Nterminal-TPR domains
experiment.sample.molecule[0].short_nameSGTA_NT-TPR
experiment.sample.molecule[0].sequenceGSMDNKKRLAYAIIQFLHDQLRHGGLSSDAQESLEVAIQCLETAFGVTVEDSDLALPQTLPEIFEAAATGKEMPQDLRSPARTPPSEEDSAEAERLKTEGNEQMKVENFEAAVHFYGKAIELNPANAVYFCNRAAAYSKLGNYAGAVQDCERAICIDPAYSKAYGRMGLALSSLNKHVEAVAYYKKALELDPDNETYKSNLKIAELKLREAPSPT
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeO43765
experiment.sample.molecule[0].uniprot_range_first1
experiment.sample.molecule[0].uniprot_range_last213
experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMDNKKRLAYAIIQFLHDQLRHGGLSSDAQESLEVAIQCLETAFGVTVEDSDLALPQTLPE IFEAAATGKEMPQDLRSPARTPPSEEDSAEAERLKTEGNEQMKVENFEAAVHFYGKAIEL NPANAVYFCNRAAAYSKLGNYAGAVQDCERAICIDPAYSKAYGRMGLALSSLNKHVEAVA YYKKALELDPDNETYKSNLKIAELKLREAPSPTGGVGSFDIAGLLNNPGFMSMASNLMNN PQIQQLMSGMISGGNNPLGTPGTSPSQNDLASLIQAGQQFAQQMQQQNPELIEQLRSQIR SRTPSASNDDQQE
experiment.sample.molecule[0].mw23.592
experiment.sample.molecule[0].total_mw47.184
experiment.sample.molecule[0].number_molecules2
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.name10 mM potassium phosphate, 100 mM NaCl
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph6.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameSmall glutamine-rich tetratricopeptide repeat-containing protein alpha (N-terminal-TPR domains; SGTA_NT)
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].addressLondon, UK
experiment.contributor[0].affiliation[0].full_nameKing's College London
experiment.contributor[0].affiliation[0].webpagehttps://www.kcl.ac.uk
experiment.contributor[0].contributor_nameRivka
experiment.contributor[0].contributor_surnameIsaacson
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
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experiment.storage_temperaturenull
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fits[]
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pddf_softwarenull
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i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from solutions of the small glutamine-rich tetratricopeptide repeat-containing protein alpha (N-terminal-TPR domains; SGTA_NT) in 10 mM potassium phosphate, 100 mM NaCl, pH 6, were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY, Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.6 and 4.5 mg/ml were measured at 25°C. 20 successive 0.045 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.
tags[]
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guinier_i010844.0
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guinier_point_last128
pddf_point_firstnull
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i0_calibration_standard_datanull
intensities_log_log_plotSASDDC6_datloglog_img.png
symmetrynull
last_modified2023-06-21T07:56:39.492710+02:00
bragg_peak[]
manifest.json:33 field values
Field pathRaw value
codeSASDDC6
statussuccess
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finished_at2026-08-11T15:06:17.505395+00:00
source_last_modified2023-06-21T07:56:39.492710+02:00
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View the complete summary.json source
{
  "code": "SASDDC6",
  "status": "Published",
  "type_of_curve": "Merged",
  "angular_unit": "1/nm",
  "project": {
    "title": "Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control.",
    "publication": {
      "title": "Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control.",
      "author_list": "Martínez-Lumbreras S, Krysztofinska EM, Thapaliya A, Spilotros A, Matak-Vinkovic D, Salvadori E, Roboti P, Nyathi Y, Muench JH, Roessler MM, Svergun DI, High S, Isaacson RL",
      "journal": "BMC Biol",
      "doi": "10.1186/s12915-018-0542-3",
      "pmid": "29996828",
      "published_date": "2018 Jul 11"
    },
    "status": "released",
    "submitted_date": "2018-05-02",
    "released_date": "2018-06-11"
  },
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          "long_name": "Small glutamine-rich tetratricopeptide repeat-containing protein alpha Nterminal-TPR domains",
          "short_name": "SGTA_NT-TPR",
          "sequence": "GSMDNKKRLAYAIIQFLHDQLRHGGLSSDAQESLEVAIQCLETAFGVTVEDSDLALPQTLPEIFEAAATGKEMPQDLRSPARTPPSEEDSAEAERLKTEGNEQMKVENFEAAVHFYGKAIELNPANAVYFCNRAAAYSKLGNYAGAVQDCERAICIDPAYSKAYGRMGLALSSLNKHVEAVAYYKKALELDPDNETYKSNLKIAELKLREAPSPT",
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}
View the complete manifest.json source
{
  "code": "SASDDC6",
  "status": "success",
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