SASDC75

Leishmania braziliensis SGT co-chaperone

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

Sample 1 · Leishmania braziliensis SGT co-chaperone

Concentration1.5 – 6.0 Buffer / pH20 mM Potassium Phosphate, 100 mM KCl, 10 mM EDTA, 1 mM B-mercaptoethanol / 7.5
Experimental temperature20.0 Facility / beamlineBrazilian Synchrotron Light Laboratory / SAXS2 Beamline
Wavelength0.1488 nmExposure300.0 s × 3

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
SGT protein
View sequence
GSHMEEKDQPITDDHRKLVFSFLRMMRRSKVENPERTEAVAQMLGEEFGVDPAGSGGLHDTEVDVLEAFKTALREHERRSGAEQDEKFMSFVELLEKKGYFKGVEKGSDEYAQRLEKARDKFNQRNNPYEGLTAEQIKNKGNELMSQAKYKEAIAYYTKAIELESDNAVFFANRAAAHTHLKDYSNAIIDCERAIVINPEYSKSYSRLGTALFYQENYARAVEAFTKACDLDPDNDTYKEDLKRAEEKAKMTGLTTGGGMGGFPGMGGFPGMGGMPDMSQFASMMNNPQFMETAQRMMQNPEFSNMVANMAGKFSQGGMDPAELNRLGADMGMRNVDEEGNVVTPFGKVNRAAIEKLQEEEVRKNPKLAGIMADVQANGYGAFQKYLGDPDVMSLMMKFQSLMFTNPNSSA
proteinLeishmania braziliensisA4HIK6—–—dimerMolecule count 245.935 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1239[2]0.1538329–3.329362 1/nmNo uncertainty columnMissing 2390sasbdb/entries/75/sasdc75/source/SASDC75.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)17.05.0nm
i0Guinier0.06590720.00039—
i0P(r)0.066310.00296—
mwExperimental91.0—kDa
mwGuinier I(0)102.04.0kDa
rgGuinier4.480.4nm
rgP(r)4.660.3nm

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 Potassium Phosphate, 100 mM KCl, 10 mM EDTA, 1 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 date2014-05-14Storage / measurement temperature4.0 / 20.0
Exposure time300.0Frames3
Wavelength0.1488Sample-to-detector distance1.0
SourceX-ray synchrotronDetectorMAR 165 CCD
Facility / beamlineBrazilian Synchrotron Light Laboratory / SAXS2 Beamline · Campinas, Brazil
q range0.154 – 3.329Sample 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:156 field values
Field pathRaw value
codeSASDC75
statusPublished
type_of_curveMerged
angular_unit1/nm
project.titleStructural and functional studies of the Leishmania braziliensis SGT co-chaperone indicate that it shares structural features with HIP and can interact with both Hsp90 and Hsp70 with similar affinities.
project.publication.titleStructural and functional studies of the Leishmania braziliensis SGT co-chaperone indicate that it shares structural features with HIP and can interact with both Hsp90 and Hsp70 with similar affinities.
project.publication.author_listCoto ALS, Seraphim TV, Batista FAH, Dores-Silva PR, Barranco ABF, Teixeira FR, Gava LM, Borges JC
project.publication.journalInt J Biol Macromol
project.publication.doi10.1016/j.ijbiomac.2018.06.123
project.publication.pmid29959008
project.publication.published_date2018 Oct 15
project.statusreleased
project.submitted_date2017-06-17
project.released_date2018-07-03
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDC75.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDC75.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDC75_dat_img.png
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pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDC75_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDC75_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDC75.sascif
experiment.instrument.detector.typenull
experiment.instrument.detector.nameMAR 165 CCD
experiment.instrument.detector.resolutionnull
experiment.instrument.nameBrazilian Synchrotron Light Laboratory
experiment.instrument.cityCampinas
experiment.instrument.countryBrazil
experiment.instrument.beamline_nameSAXS2 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_nameSGT protein
experiment.sample.molecule[0].short_nameLbSGT
experiment.sample.molecule[0].sequenceGSHMEEKDQPITDDHRKLVFSFLRMMRRSKVENPERTEAVAQMLGEEFGVDPAGSGGLHDTEV DVLEAFKTALREHERRSGAEQDEKFMSFVELLEKKGYFKGVEKGSDEYAQRLEKARDKFN QRNNPYEGLTAEQIKNKGNELMSQAKYKEAIAYYTKAIELESDNAVFFANRAAAHTHLKD YSNAIIDCERAIVINPEYSKSYSRLGTALFYQENYARAVEAFTKACDLDPDNDTYKEDLK RAEEKAKMTGLTTGGGMGGFPGMGGFPGMGGMPDMSQFASMMNNPQFMETAQRMMQNPEF SNMVANMAGKFSQGGMDPAELNRLGADMGMRNVDEEGNVVTPFGKVNRAAIEKLQEEEVR KNPKLAGIMADVQANGYGAFQKYLGDPDVMSLMMKFQSLMFTNPNSSA
experiment.sample.molecule[0].organismLeishmania braziliensis
experiment.sample.molecule[0].uniprot_codeA4HIK6
experiment.sample.molecule[0].uniprot_range_firstnull
experiment.sample.molecule[0].uniprot_range_lastnull
experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMEEKDQPITDDHRKLVFSFLRMMRRSKVENPERTEAVAQMLGEEFGVDPAGSGGLHDTEV DVLEAFKTALREHERRSGAEQDEKFMSFVELLEKKGYFKGVEKGSDEYAQRLEKARDKFN QRNNPYEGLTAEQIKNKGNELMSQAKYKEAIAYYTKAIELESDNAVFFANRAAAHTHLKD YSNAIIDCERAIVINPEYSKSYSRLGTALFYQENYARAVEAFTKACDLDPDNDTYKEDLK RAEEKAKMTGLTTGGGMGGFPGMGGFPGMGGMPDMSQFASMMNNPQFMETAQRMMQNPEF SNMVANMAGKFSQGGMDPAELNRLGADMGMRNVDEEGNVVTPFGKVNRAAIEKLQEEEVR KNPKLAGIMADVQANGYGAFQKYLGDPDVMSLMMKFQSLMFTNPNSSA
experiment.sample.molecule[0].mw45.935
experiment.sample.molecule[0].total_mw91.87
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.name20 mM Potassium Phosphate, 100 mM KCl, 10 mM EDTA, 1 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.nameLeishmania braziliensis SGT co-chaperone
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.date2014-05-14
experiment.storage_temperature4.0
experiment.cell_temperature20.0
experiment.exposure_time300.0
experiment.number_of_frames3
experiment.wavelength0.1488
experiment.sample_detector_distance1.0
experiment.concentration_min1.5
experiment.concentration_max6.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.154
experiment.s_max3.329
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].softwareDAMFILT
fits[0].models[0].pdb_link[]
fits[0].models[0].model_titlenull
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fits[0].models[0].symmetryP2
fits[0].models[0].comment
fits[0].models[0].user161
fits[0].fit_unit1/A
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fits[0].softwareDAMMIN
fits[0].chi_square_value1.476
fits[0].p_value0.203609
fits[0].fit_residual_plotSASDC75_fit1_fitresiduals_img.png
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fits[0].software_version5.3
fits[0].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version4.6
i0_calibration_standardnull
descriptionnull
experiment_descriptionSAXS experiments were performed at the D02A-SAXS2 beamline at the Brazilian Synchrotron Light Laboratory (LNLS, Campinas, São Paulo, Brazil). The X-ray scattering data (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle; λ = 0.1488 nm) were acquired using a two-dimensional position-sensitive MAR-CCD detector. Measurements were performed using a monochromatic X-ray beam and a sample-to-detector distance of ~1,000 mm, corresponding to the scattering vector range of 0.015 < q < 0.35 Å-1. LbSGT samples were prepared at 1.5 mg/mL, 3.0 mg/mL, 4.5 mg/mL and 6.0 mg/mL. Successive frames (20, 60 and 300 sec) were collected to inspect for X-ray damage. Aggregation or inter-particle interference were not observed. The model depicts the averaged spatial representation of the protein (DAMFILT occupancy and volume-corrected bead model).
tags[]
intensity_unitnull
experimental_mw91.0
experimental_mw_errornull
guinier_i0_mw102.0
guinier_i0_mw_error4.0
porod_mwnull
porod_mw_errornull
pddf_i00.06631
pddf_i0_error0.00296
guinier_i00.0659072
guinier_i0_error0.00039
pddf_rg4.66
pddf_rg_error0.3
guinier_rg4.48
guinier_rg_error0.4
pddf_dmax17.0
pddf_dmax_error5.0
porod_volumenull
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first2
guinier_point_last11
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDC75_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDC75
statussuccess
started_at2026-08-11T14:40:48.175875+00:00
finished_at2026-08-11T14:40:55.629428+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDC75",
  "status": "Published",
  "type_of_curve": "Merged",
  "angular_unit": "1/nm",
  "project": {
    "title": "Structural and functional studies of the Leishmania braziliensis SGT co-chaperone indicate that it shares structural features with HIP and can interact with both Hsp90 and Hsp70 with similar affinities.",
    "publication": {
      "title": "Structural and functional studies of the Leishmania braziliensis SGT co-chaperone indicate that it shares structural features with HIP and can interact with both Hsp90 and Hsp70 with similar affinities.",
      "author_list": "Coto ALS, Seraphim TV, Batista FAH, Dores-Silva PR, Barranco ABF, Teixeira FR, Gava LM, Borges JC",
      "journal": "Int J Biol Macromol",
      "doi": "10.1016/j.ijbiomac.2018.06.123",
      "pmid": "29959008",
      "published_date": "2018 Oct 15"
    },
    "status": "released",
    "submitted_date": "2017-06-17",
    "released_date": "2018-07-03"
  },
  "pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDC75.out",
  "intensities_data": "https://www.sasbdb.org/media/intensities_files/SASDC75.dat",
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  "experiment": {
    "instrument": {
      "detector": {
        "type": null,
        "name": "MAR 165 CCD",
        "resolution": null
      },
      "name": "Brazilian Synchrotron Light Laboratory",
      "city": "Campinas",
      "country": "Brazil",
      "beamline_name": "SAXS2 Beamline",
      "beam_geometry": "",
      "type_of_source": "X-ray synchrotron",
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      "line_collimation": null,
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      "xray_energy": null,
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    },
    "sample": {
      "molecule": [
        {
          "long_name": "SGT protein",
          "short_name": "LbSGT",
          "sequence": "GSHMEEKDQPITDDHRKLVFSFLRMMRRSKVENPERTEAVAQMLGEEFGVDPAGSGGLHDTEV\r\nDVLEAFKTALREHERRSGAEQDEKFMSFVELLEKKGYFKGVEKGSDEYAQRLEKARDKFN\r\nQRNNPYEGLTAEQIKNKGNELMSQAKYKEAIAYYTKAIELESDNAVFFANRAAAHTHLKD\r\nYSNAIIDCERAIVINPEYSKSYSRLGTALFYQENYARAVEAFTKACDLDPDNDTYKEDLK\r\nRAEEKAKMTGLTTGGGMGGFPGMGGFPGMGGMPDMSQFASMMNNPQFMETAQRMMQNPEF\r\nSNMVANMAGKFSQGGMDPAELNRLGADMGMRNVDEEGNVVTPFGKVNRAAIEKLQEEEVR\r\nKNPKLAGIMADVQANGYGAFQKYLGDPDVMSLMMKFQSLMFTNPNSSA",
          "organism": "Leishmania braziliensis",
          "uniprot_code": "A4HIK6",
          "uniprot_range_first": null,
          "uniprot_range_last": null,
          "oligomerization": "dimer",
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          "uniprot_sequence": "MEEKDQPITDDHRKLVFSFLRMMRRSKVENPERTEAVAQMLGEEFGVDPAGSGGLHDTEV\nDVLEAFKTALREHERRSGAEQDEKFMSFVELLEKKGYFKGVEKGSDEYAQRLEKARDKFN\nQRNNPYEGLTAEQIKNKGNELMSQAKYKEAIAYYTKAIELESDNAVFFANRAAAHTHLKD\nYSNAIIDCERAIVINPEYSKSYSRLGTALFYQENYARAVEAFTKACDLDPDNDTYKEDLK\nRAEEKAKMTGLTTGGGMGGFPGMGGFPGMGGMPDMSQFASMMNNPQFMETAQRMMQNPEF\nSNMVANMAGKFSQGGMDPAELNRLGADMGMRNVDEEGNVVTPFGKVNRAAIEKLQEEEVR\nKNPKLAGIMADVQANGYGAFQKYLGDPDVMSLMMKFQSLMFTNPNSSA",
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View the complete manifest.json source
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