SASDBP9

Human Hsp90 co-chaperone Cdc37 protein (CD37)

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

Sample 1 · Human Hsp90 co-chaperone Cdc37 protein (CD37)

Concentration1.1 – 4.2 Buffer / pH25 mM Tris.Cl, 150 mM NaCl, 5% (v/v) glycerol, 1 mM TCEP / 8.0
Experimental temperature20.0 Facility / beamlinePETRA III / EMBL P12
Wavelength0.124 nmExposure0.045 s × 20

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Hsp90 co-chaperone Cdc37
View sequence
MVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAEGGKAELERLQAEAQQLRKEERSWEQKLEEMRKKEKSMPWNVDTLSKDGFSKSMVNTKPEKTEEDSEEVREQKHKTFVEKYEKQIKHFGMLRRWDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALMEQVAHQTIVMQFILELAKSLKVDPRACFRQFFTKIKTADRQYMEGFNDELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLDPVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKASEAKEGEEAGPGDPLLEAVPKTGDEKDGSV
proteinHomo sapiensQ16543—–—monomerMolecule count 144.426 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11818[3]0.0247955–5.0307 1/nmHas uncertainty columnMissing 024sasbdb/entries/p9/sasdbp9/source/SASDBP9.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)15.533.0nm
i0Guinier5968.7417.13—
i0P(r)6042.018.03—
mwExperimental49.1—kDa
mwGuinier I(0)49.15.0kDa
mwPorod52.0—kDa
porod_volumePorod106.46—nm³
rgGuinier3.990.59nm
rgP(r)4.190.02nm

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 name25 mM Tris.Cl, 150 mM NaCl, 5% (v/v) glycerol, 1 mM TCEPBuffer concentration—
pH8.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2016-07-10Storage / measurement temperature20.0 / 20.0
Exposure time0.045Frames20
Wavelength0.124Sample-to-detector distance3.1
SourceX-ray synchrotronDetectorPilatus 2M
Facility / beamlinePETRA III / EMBL P12 · DESY; Hamburg, Germany
q range0.025 – 5.031Sample 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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full_entry_zip:source record and ZIP contents (6 items)
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pddf: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:182 field values
Field pathRaw value
codeSASDBP9
statusPublished
type_of_curveExtrapolated to infinite dilution
angular_unit1/nm
project.titleDisease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System.
project.publication.titleDisease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System.
project.publication.author_listBunney TD, Inglis AJ, Sanfelice D, Farrell B, Kerr CJ, Thompson GS, Masson GR, Thiyagarajan N, Svergun DI, Williams RL, Breeze AL, Katan M
project.publication.journalStructure
project.publication.doi10.1016/j.str.2018.01.016
project.publication.pmid29478821
project.publication.published_date2018 Mar 6
project.statusreleased
project.submitted_date2017-01-18
project.released_date2018-03-20
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sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDBP9.sascif
experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus 2M
experiment.instrument.detector.resolutionnull
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
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_nameHsp90 co-chaperone Cdc37
experiment.sample.molecule[0].short_nameCDC37
experiment.sample.molecule[0].sequenceMVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRK VAECQRKLKELEVAEGGKAELERLQAEAQQLRKEERSWEQKLEEMRKKEKSMPWNVDTLS KDGFSKSMVNTKPEKTEEDSEEVREQKHKTFVEKYEKQIKHFGMLRRWDDSQKYLSDNVH LVCEETANYLVIWCIDLEVEEKCALMEQVAHQTIVMQFILELAKSLKVDPRACFRQFFTK IKTADRQYMEGFNDELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLDPVEVYES LPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKASEAKEGEEAGPG DPLLEAVPKTGDEKDGSV
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeQ16543
experiment.sample.molecule[0].uniprot_range_firstnull
experiment.sample.molecule[0].uniprot_range_lastnull
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRK VAECQRKLKELEVAEGGKAELERLQAEAQQLRKEERSWEQKLEEMRKKEKSMPWNVDTLS KDGFSKSMVNTKPEKTEEDSEEVREQKHKTFVEKYEKQIKHFGMLRRWDDSQKYLSDNVH LVCEETANYLVIWCIDLEVEEKCALMEQVAHQTIVMQFILELAKSLKVDPRACFRQFFTK IKTADRQYMEGFNDELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLDPVEVYES LPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKASEAKEGEEAGPG DPLLEAVPKTGDEKDVSV
experiment.sample.molecule[0].mw44.426
experiment.sample.molecule[0].total_mw44.426
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.Cl, 150 mM NaCl, 5% (v/v) glycerol, 1 mM TCEP
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.nameHuman Hsp90 co-chaperone Cdc37 protein (CD37)
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_nameEMBL-Hamburg
experiment.contributor[0].affiliation[0].addressNotkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany
experiment.contributor[0].affiliation[0].full_nameEuropean Molecular Biology Laboratory (EMBL) - Hamburg outstation
experiment.contributor[0].affiliation[0].webpagehttp://www.embl-hamburg.de/index.php
experiment.contributor[0].contributor_nameChris
experiment.contributor[0].contributor_surnameKerr
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2016-07-10
experiment.storage_temperature20.0
experiment.cell_temperature20.0
experiment.exposure_time0.045
experiment.number_of_frames20
experiment.wavelength0.124
experiment.sample_detector_distance3.1
experiment.concentration_min1.1
experiment.concentration_max4.2
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.025
experiment.s_max5.031
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].pdb_link[0].pdb_code1us7
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fits[0].models[0].bead_radius1.9
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fits[0].softwareCORAL
fits[0].chi_square_value1.88
fits[0].p_value0.0
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fits[0].descriptionnull
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fits[1].models[0].comment
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fits[1].fit_unit1/A
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fits[1].softwareMONSA
fits[1].chi_square_value1.635
fits[1].p_value0.0
fits[1].fit_residual_plotSASDBP9_fit2_fitresiduals_img.png
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fits[1].software_versionATSAS2.7.2
fits[1].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionGNOM5 - trunk r8992
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from solutions of human Hsp90 co-chaperone Cdc37 protein (CD37) in 25 mM Tris-HCl, 150 mM NaCl, 5% (v/v) glycerol, 1 mM TCEP, pH 8, were collected on the P12 beam line at the PETRA III storage ring (Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.1 and 4.2 mg/ml were measured at 20°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 and the different curves were scaled for protein concentration. The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.
tags[]
intensity_unitnull
experimental_mw49.1
experimental_mw_errornull
guinier_i0_mw49.1
guinier_i0_mw_error5.0
porod_mw52.0
porod_mw_errornull
pddf_i06042.0
pddf_i0_error18.03
guinier_i05968.74
guinier_i0_error17.13
pddf_rg4.19
pddf_rg_error0.02
guinier_rg3.99
guinier_rg_error0.59
pddf_dmax15.53
pddf_dmax_error3.0
porod_volume106.46
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first25
guinier_point_last110
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDBP9_datloglog_img.png
symmetrynull
last_modified2023-06-21T07:56:39.492710+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDBP9
statussuccess
started_at2026-08-11T16:19:01.354279+00:00
finished_at2026-08-11T16:19:13.065156+00:00
source_last_modified2023-06-21T07:56:39.492710+02:00
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View the complete summary.json source
{
  "code": "SASDBP9",
  "status": "Published",
  "type_of_curve": "Extrapolated to infinite dilution",
  "angular_unit": "1/nm",
  "project": {
    "title": "Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System.",
    "publication": {
      "title": "Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System.",
      "author_list": "Bunney TD, Inglis AJ, Sanfelice D, Farrell B, Kerr CJ, Thompson GS, Masson GR, Thiyagarajan N, Svergun DI, Williams RL, Breeze AL, Katan M",
      "journal": "Structure",
      "doi": "10.1016/j.str.2018.01.016",
      "pmid": "29478821",
      "published_date": "2018 Mar 6"
    },
    "status": "released",
    "submitted_date": "2017-01-18",
    "released_date": "2018-03-20"
  },
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  "experiment": {
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      "detector": {
        "type": null,
        "name": "Pilatus 2M",
        "resolution": null
      },
      "name": "PETRA III",
      "city": "DESY; Hamburg",
      "country": "Germany",
      "beamline_name": "EMBL P12",
      "beam_geometry": null,
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            "address": "Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany",
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View the complete manifest.json source
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