SASDB94

Suppressor of Copper Sensitivity C protein (ScsC) from Proteus mirabilis

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2020-08-28T15:27:57.490687+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Suppressor of Copper Sensitivity C protein (ScsC) from Proteus mirabilis

Concentration2.15 – 8.85 Buffer / pH25 mM HEPES 150mM NaCl 1mM DTT / 7.5
Experimental temperature10.0 Facility / beamlineAustralian Synchrotron / SAXS/WAXS
Wavelength— nmExposure2.0 s × 14

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein
View sequence
SNAQFRQALASEHDALYNDAASPRIGAKDAKLVLVSFTDYNCPYCKRFDPLLEKITEQYPDVAVIIKPLPFKGESSAKASQAVLSVWKEDPKAFLALHQRLMQKKTMLDNASIEDAMKSTNTSKIKLTDDSLKTLQNNLELSRKLGIQGTPATVIGDTILPGAVDYDQLEIIVKEQLAKVKK
proteinProteus mirabilisA0A1Z1SYD564–243monomerMolecule count 120.15 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1182[3]0.0862801–2.48729 1/nmHas uncertainty columnMissing 00sasbdb/entries/94/sasdb94/source/SASDB94.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)10.5—nm
i0Guinier0.101——
i0P(r)0.10060.00016—
mwExperimental69.9—kDa
porod_volumePorod92.0—nm³
rgGuinier3.65—nm
rgP(r)3.60.01nm

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 150mM NaCl 1mM DTTBuffer concentration25.0 mM
pH7.5Additives150mM NaCl, 1mM DTT
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2012-02-29Storage / measurement temperature10.0 / 10.0
Exposure time2.0Frames14
Wavelength—Sample-to-detector distance1.6
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineAustralian Synchrotron / SAXS/WAXS · Melbourne, Australia
q range0.086 – 2.487Sample 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:247 field values
Field pathRaw value
codeSASDB94
statusPublished
type_of_curveSingle concentration
angular_unit1/nm
project.titleA shape-shifting redox foldase contributes to Proteus mirabilis copper resistance.
project.publication.titleA shape-shifting redox foldase contributes to Proteus mirabilis copper resistance.
project.publication.author_listFurlong EJ, Lo AW, Kurth F, Premkumar L, Totsika M, Achard MES, Halili MA, Heras B, Whitten AE, Choudhury HG, Schembri MA, Martin JL
project.publication.journalNat Commun
project.publication.doi10.1038/ncomms16065
project.publication.pmid28722010
project.publication.published_date2017 Jul 19
project.statusreleased
project.submitted_date2016-10-04
project.released_date2017-06-16
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experiment.instrument.detector.typeDectris
experiment.instrument.detector.namePilatus 1M
experiment.instrument.detector.resolution172.0
experiment.instrument.nameAustralian Synchrotron
experiment.instrument.cityMelbourne
experiment.instrument.countryAustralia
experiment.instrument.beamline_nameSAXS/WAXS
experiment.instrument.beam_geometryPoint
experiment.instrument.type_of_sourceX-ray synchrotron
experiment.instrument.point_sourceTrue
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_nameC-terminal catalytic domain of Suppressor of Copper Sensitivity C protein
experiment.sample.molecule[0].short_namePmScsCΔN
experiment.sample.molecule[0].sequenceSNAQFRQALASEHDALYNDAASPRIGAKDAKLVLVSFTDYNCPYCKRFDPLLEKITEQYPDVAVIIKPLPFKGESSAKASQAVLSVWKEDPKAFLALHQRLMQKKTMLDNASIEDAMKSTNTSKIKLTDDSLKTLQNNLELSRKLGIQGTPATVIGDTILPGAVDYDQLEIIVKEQLAKVKK
experiment.sample.molecule[0].organismProteus mirabilis
experiment.sample.molecule[0].uniprot_codeA0A1Z1SYD5
experiment.sample.molecule[0].uniprot_range_first64
experiment.sample.molecule[0].uniprot_range_last243
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMKKTLSVLVISSLLFGANVQAAALNAAQEKEVRALVRDTLVSNPEILEEAIMALQTKKAD EQQAQFRQALASEHDALYNDAASPRIGAKDAKLVLVSFTDYNCPYCKRFDPLLEKITEQY PDVAVIIKPLPFKGESSAKASQAVLSVWKEDPKAFLALHQRLMQKKTMLDNASIEDAMKS TNTSKIKLTDDSLKTLQNNLELSRKLGIQGTPATVIGDTILPGAVDYDQLEIIVKEQLAK VKK
experiment.sample.molecule[0].mw20.15
experiment.sample.molecule[0].total_mw20.15
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 HEPES 150mM NaCl 1mM DTT
experiment.sample.buffer.concentration_unitmM
experiment.sample.buffer.commentnull
experiment.sample.buffer.additive150mM NaCl, 1mM 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.nameSuppressor of Copper Sensitivity C protein (ScsC) from Proteus mirabilis
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_nameANSTO
experiment.contributor[0].affiliation[0].addressKirrawee DC, NSW 2232, Australia
experiment.contributor[0].affiliation[0].full_nameAustralian Nuclear Science and Technology Organisation
experiment.contributor[0].affiliation[0].webpage
experiment.contributor[0].contributor_nameAndrew
experiment.contributor[0].contributor_surnameWhitten
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2012-02-29
experiment.storage_temperature10.0
experiment.cell_temperature10.0
experiment.exposure_time2.0
experiment.number_of_frames14
experiment.wavelengthnull
experiment.sample_detector_distance1.6
experiment.concentration_min2.15
experiment.concentration_max8.85
experiment.sample_volumenull
experiment.flow_ratenull
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experiment.total_exposure_timenull
experiment.seccolumnnull
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pddf_softwareATSAS GNOM
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i0_calibration_standardnull
descriptionnull
experiment_descriptionX-ray synchrotron radiation scattering data from solutions of Suppressor of Copper Sensitivity C protein (ScsC) from Proteus mirabilis in 25 mM HEPES 150mM NaCl, 1mM DTT, pH 7.5 were collected on the SAXS/WAXS beam line of the Australian Synchrotron (Melbourne, Australia) using a 2D Photon counting Pilatus 1M-W pixel detector (s = 4π sin θ/λ, where 2θ is the scattering angle). Fourteen successive 2 second frames were collected across solute concentrations of 2.15-8.85 mg/ml. The SAXS data displayed this entry was derived from a 2.15 mg/ml sample. The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted. The models and corresponding fits include those derived from rigid-body modelling using CORAL (top) and a representative ensemble of six trimeric ScsC structures determined using ensemble optimization method (EOM). The Rg and Dmax distributions derived from EOM are included in the full entry zip archive.
tags[]
intensity_unitnull
experimental_mw69.9
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i00.1006
pddf_i0_error0.00016
guinier_i00.101
guinier_i0_errornull
pddf_rg3.6
pddf_rg_error0.01
guinier_rg3.65
guinier_rg_errornull
pddf_dmax10.5
pddf_dmax_errornull
porod_volume92.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first3
guinier_point_last21
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDB94_datloglog_img.png
symmetrynull
last_modified2020-08-28T15:27:57.490687+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDB94
statussuccess
started_at2026-08-11T14:16:30.520236+00:00
finished_at2026-08-11T14:16:42.170445+00:00
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View the complete summary.json source
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    "title": "A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance.",
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      "title": "A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance.",
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View the complete manifest.json source
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