SASDB45

Trimeric periplasmic holdase chaperone protein Skp

Data type: SASBDB experimental data Status: Published Curve type: Merged Last updated: 2023-06-21T07:56:39.492710+02:00

The models presented above are representatives from the trimeric ensemble state(s) of Skp as determined using Ensemble Optimization Method (EOM). The Rg and size distributions obtained from EOM modelling are included in the full entry zip archive.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Trimeric periplasmic holdase chaperone protein Skp

Concentration0.58 – 5.82 mg/mlBuffer / pH25 mM HEPES 150 mM NaCl 1 mM DTT / 7.5
Experimental temperature10.0 Facility / beamlinePETRA III / EMBL P12
Wavelength0.12 nmExposure0.05 s × 20

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Periplasmic holdase chaperone protein Skp
View sequence
ADKIAIVNMGSLFQQVAQKTGVSNTLENEFKGRASELQRMETDLQAKMKKLQSMKAGSDRTKLEKDVMAQRQTFAQKAQAFEQDRARRSNEERGKLVTRIQTAVKSVANSQDIDLVVDANAVAYNSSDVKDITADVLKQVK
proteinEscherichia coliP0AEU721–161trimerMolecule count 315.692 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11650[3]0.096949–4.43724 1/nmHas uncertainty columnMissing 00sasbdb/entries/45/sasdb45/source/SASDB45.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)12.8—nm
i0Guinier4451.754.4—
i0P(r)4369.029.7—
mwExperimental35.0—kDa
mwPorod100.0—kDa
porod_volumePorod168.0—nm³
rgGuinier3.570.07nm
rgP(r)3.570.02nm

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 HEPES 150 mM NaCl 1 mM DTTBuffer concentration25.0 mM
pH7.5Additives150 mM NaCl, 1 mM DTT
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2013-09-24Storage / measurement temperature10.0 / 10.0
Exposure time0.05Frames20
Wavelength0.12Sample-to-detector distance3.1
SourceX-ray synchrotronDetectorPilatus 2M
Facility / beamlinePETRA III / EMBL P12 · DESY; Hamburg, Germany
q range0.097 – 4.437Sample 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:182 field values
Field pathRaw value
codeSASDB45
statusPublished
type_of_curveMerged
angular_unit1/nm
project.titleA Spring-Loaded Mechanism Governs the Clamp-like Dynamics of the Skp Chaperone.
project.publication.titleA Spring-Loaded Mechanism Governs the Clamp-like Dynamics of the Skp Chaperone.
project.publication.author_listHoldbrook DA, Burmann BM, Huber RG, Petoukhov MV, Svergun DI, Hiller S, Bond PJ
project.publication.journalStructure
project.publication.doi10.1016/j.str.2017.05.018
project.publication.pmid28648612
project.publication.published_date2017 Jul 5
project.statusreleased
project.submitted_date2016-07-24
project.released_date2017-06-27
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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
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experiment.sample.molecule[0].long_namePeriplasmic holdase chaperone protein Skp
experiment.sample.molecule[0].short_nameSkp
experiment.sample.molecule[0].sequenceADKIAIVNMGSLFQQVAQKTGVSNTLENEFKGRASELQRMETDLQAKMKKLQSMKAGSDRTKLEKDVMAQRQTFAQKAQAFEQDRARRSNEERGKLVTRIQTAVKSVANSQDIDLVVDANAVAYNSSDVKDITADVLKQVK
experiment.sample.molecule[0].organismEscherichia coli
experiment.sample.molecule[0].uniprot_codeP0AEU7
experiment.sample.molecule[0].uniprot_range_first21
experiment.sample.molecule[0].uniprot_range_last161
experiment.sample.molecule[0].oligomerizationtrimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMKKWLLAAGLGLALATSAQAADKIAIVNMGSLFQQVAQKTGVSNTLENEFKGRASELQRM ETDLQAKMKKLQSMKAGSDRTKLEKDVMAQRQTFAQKAQAFEQDRARRSNEERGKLVTRI QTAVKSVANSQDIDLVVDANAVAYNSSDVKDITADVLKQVK
experiment.sample.molecule[0].mw15.692
experiment.sample.molecule[0].total_mw47.075
experiment.sample.molecule[0].number_molecules3
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 HEPES 150 mM NaCl 1 mM DTT
experiment.sample.buffer.concentration_unitmM
experiment.sample.buffer.commentnull
experiment.sample.buffer.additive150 mM NaCl, 1 mM DTT
experiment.sample.buffer.concentration25.0
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameTrimeric periplasmic holdase chaperone protein Skp
experiment.sample.ext_coefficientnull
experiment.sample.contrastnull
experiment.sample.specific_volnull
experiment.sample.dry_volnull
experiment.sample.absorbptionnull
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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_nameMaxim
experiment.contributor[0].contributor_surnamePetoukhov
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitmg/ml
experiment.date2013-09-24
experiment.storage_temperature10.0
experiment.cell_temperature10.0
experiment.exposure_time0.05
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experiment.wavelength0.12
experiment.sample_detector_distance3.1
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pddf_softwareATSAS GNOM
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i0_calibration_standardnull
descriptionThe models presented above are representatives from the trimeric ensemble state(s) of Skp as determined using Ensemble Optimization Method (EOM). The Rg and size distributions obtained from EOM modelling are included in the full entry zip archive.
experiment_descriptionX-ray synchrotron radiation scattering data from solutions of periplasmic holdase chaperone protein Skp in 25 mM HEPES 150 mM NaCl, 1 mM DTT, pH 7.5 were measured at the EMBL-P12 bioSAXS beam line on the PETRAIII storage ring (Hamburg, Germany) using a Pilatus 2M detector ((I(s) vs s, where s = 4π sin θ/λ; 2θ is the scattering angle; λ = 0.12 nm). Different solute concentrations in the range 0.58-5.82 mg/ml were measured where each sample and corresponding matched solvent blank were collected as 20 successive 50 ms frames for a total exposure time of 1 s. 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 from the 0.58 mg/ml sample were merged with the highest concentration (5.82 mg/ml) high angle data to yield the final composite scattering curve. The original SAXS data used to obtain the merged profile as displayed in this entry are included in the full entry zip archive.
tags[]
intensity_unitnull
experimental_mw35.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw100.0
porod_mw_errornull
pddf_i04369.0
pddf_i0_error29.7
guinier_i04451.7
guinier_i0_error54.4
pddf_rg3.57
pddf_rg_error0.02
guinier_rg3.57
guinier_rg_error0.07
pddf_dmax12.8
pddf_dmax_errornull
porod_volume168.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first1
guinier_point_last99
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDB45_datloglog_img.png
symmetrynull
last_modified2023-06-21T07:56:39.492710+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDB45
statussuccess
started_at2026-08-11T14:37:35.730096+00:00
finished_at2026-08-11T14:37:45.675327+00:00
source_last_modified2023-06-21T07:56:39.492710+02:00
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View the complete summary.json source
{
  "code": "SASDB45",
  "status": "Published",
  "type_of_curve": "Merged",
  "angular_unit": "1/nm",
  "project": {
    "title": "A Spring-Loaded Mechanism Governs the Clamp-like Dynamics of the Skp Chaperone.",
    "publication": {
      "title": "A Spring-Loaded Mechanism Governs the Clamp-like Dynamics of the Skp Chaperone.",
      "author_list": "Holdbrook DA, Burmann BM, Huber RG, Petoukhov MV, Svergun DI, Hiller S, Bond PJ",
      "journal": "Structure",
      "doi": "10.1016/j.str.2017.05.018",
      "pmid": "28648612",
      "published_date": "2017 Jul 5"
    },
    "status": "released",
    "submitted_date": "2016-07-24",
    "released_date": "2017-06-27"
  },
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    "sample": {
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        {
          "long_name": "Periplasmic holdase chaperone protein Skp",
          "short_name": "Skp",
          "sequence": "ADKIAIVNMGSLFQQVAQKTGVSNTLENEFKGRASELQRMETDLQAKMKKLQSMKAGSDRTKLEKDVMAQRQTFAQKAQAFEQDRARRSNEERGKLVTRIQTAVKSVANSQDIDLVVDANAVAYNSSDVKDITADVLKQVK",
          "organism": "Escherichia coli",
          "uniprot_code": "P0AEU7",
          "uniprot_range_first": 21,
          "uniprot_range_last": 161,
          "oligomerization": "trimer",
          "molecular_type": "protein",
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            "short_name": "EMBL-Hamburg",
            "address": "Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany",
            "full_name": "European Molecular Biology Laboratory (EMBL) - Hamburg outstation",
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View the complete manifest.json source
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