SASDEW7

C-terminal truncated bank vole prion protein (amino acids 90-231)

Data type: SASBDB experimental data Status: Published Curve type: SEC-SAS Last updated: 2020-08-28T15:28:09.828046+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · C-terminal truncated bank vole prion protein (amino acids 90-231)

Concentration— – 10.0 Buffer / pH25 mM Ammonium Acetate, 250 mM NaCl / 5.5
Experimental temperature20.0 Facility / beamlineESRF / BM29
Wavelength0.099 nmExposure1.0 s × 1

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Major prion protein
View sequence
GQGGGTHNQWNKPSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMNRYPNQVYYRPVDQYNNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYEGRSS
proteinMyodes glareolusQ8VHV590–231monomerMolecule count 116.14 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11029[3]0.1029623–4.927702 1/nmHas uncertainty columnMissing 040sasbdb/entries/w7/sasdew7/source/SASDEW7.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)9.4—nm
i0Guinier25.070.05arbitrary
i0P(r)25.62—arbitrary
mwExperimental16.1—kDa
mwGuinier I(0)16.30.0kDa
mwPorod14.3—kDa
porod_volumePorod28.54—nm³
rgGuinier2.250.01nm
rgP(r)2.417—nm

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 Ammonium Acetate, 250 mM NaClBuffer concentration—
pH5.5Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2018-02-25Storage / measurement temperature20.0 / 20.0
Exposure time1.0Frames1
Wavelength0.099Sample-to-detector distance2.864
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineESRF / BM29 · Grenoble, France
q range0.103 – 4.928Sample 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

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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
codeSASDEW7
statusPublished
type_of_curveSEC-SAS
angular_unit1/nm
project.titleDeciphering Copper Coordination in the Mammalian Prion Protein Amyloidogenic Domain
project.publication.titleDeciphering Copper Coordination in the Mammalian Prion Protein Amyloidogenic Domain
project.publication.author_listSalzano G, Brennich M, Mancini G, Tran T, Legname G, D’Angelo P, Giachin G
project.publication.journalBiophysical Journal
project.publication.doi10.1016/j.bpj.2019.12.025
project.publication.pmidnull
project.publication.published_date2020 Jan
project.statusreleased
project.submitted_date2018-11-13
project.released_date2019-11-25
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experiment.instrument.detector.namePilatus 1M
experiment.instrument.detector.resolution172.0
experiment.instrument.nameESRF
experiment.instrument.cityGrenoble
experiment.instrument.countryFrance
experiment.instrument.beamline_nameBM29
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_nameMajor prion protein
experiment.sample.molecule[0].short_namenull
experiment.sample.molecule[0].sequenceGQGGGTHNQWNKPSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMNRYPNQVYYRPVDQYNNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYEGRSS
experiment.sample.molecule[0].organismMyodes glareolus
experiment.sample.molecule[0].uniprot_codeQ8VHV5
experiment.sample.molecule[0].uniprot_range_first90
experiment.sample.molecule[0].uniprot_range_last231
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMANLSYWLLAFFVTTWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQP HGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHVAGAAAAGA VVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMNRYPNQVYYRPVDQYNNQNNFVHDCV NITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYEGRSSRAVLLFSSP PVILLISF
experiment.sample.molecule[0].mw16.14
experiment.sample.molecule[0].total_mw16.14
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 Ammonium Acetate, 250 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.ph5.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameC-terminal truncated bank vole prion protein (amino acids 90-231)
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_nameESRF
experiment.contributor[0].affiliation[0].addressGrenoble, France
experiment.contributor[0].affiliation[0].full_nameEuropean Synchrotron Radiation Facility
experiment.contributor[0].affiliation[0].webpagehttp://www.esrf.eu/
experiment.contributor[0].contributor_nameGabriele
experiment.contributor[0].contributor_surnameGiachin
experiment.contributor[0].orcidhttps://orcid.org/0000-0001-7550-0307
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2018-02-25
experiment.storage_temperature20.0
experiment.cell_temperature20.0
experiment.exposure_time1.0
experiment.number_of_frames1
experiment.wavelength0.099
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experiment.concentration_max10.0
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experiment.flow_ratenull
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experiment.total_exposure_timenull
experiment.seccolumnnull
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pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from solutions of the C-terminal truncated bank vole prion protein (amino acids 90-231) in 25 mM ammonium acetate, 250 mM NaCl, pH 5.5 were collected using size exclusion chromatography SAXS (SEC-SAXS) on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.099 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). SEC-SAXS was performed at 20 °C using the following parameters: Column type, Superdex 75 10/300 GL (GE Healthcare); Flow rate: 0.5 mL/min; Total acquisition time: 50 min; Injection concentration: 10 mg/mL; Injection volume: 250 μL. The data obtained through the sample elution peak (1963-2030 1 s frames) were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the individual subtracted data sets were scaled and averaged to generate the scattering profile displayed in this entry.
tags[]
intensity_unitarbitrary
experimental_mw16.1
experimental_mw_errornull
guinier_i0_mw16.3
guinier_i0_mw_error0.0
porod_mw14.3
porod_mw_errornull
pddf_i025.62
pddf_i0_errornull
guinier_i025.07
guinier_i0_error0.05
pddf_rg2.417
pddf_rg_errornull
guinier_rg2.25
guinier_rg_error0.01
pddf_dmax9.4
pddf_dmax_errornull
porod_volume28.54
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first35
guinier_point_last70
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDEW7_datloglog_img.png
symmetrynull
last_modified2020-08-28T15:28:09.828046+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDEW7
statussuccess
started_at2026-08-11T15:41:16.286584+00:00
finished_at2026-08-11T15:41:27.119591+00:00
source_last_modified2020-08-28T15:28:09.828046+02:00
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View the complete summary.json source
{
  "code": "SASDEW7",
  "status": "Published",
  "type_of_curve": "SEC-SAS",
  "angular_unit": "1/nm",
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    "title": "Deciphering Copper Coordination in the Mammalian Prion Protein Amyloidogenic Domain",
    "publication": {
      "title": "Deciphering Copper Coordination in the Mammalian Prion Protein Amyloidogenic Domain",
      "author_list": "Salzano G, Brennich M, Mancini G, Tran T, Legname G, D’Angelo P, Giachin G",
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      "doi": "10.1016/j.bpj.2019.12.025",
      "pmid": null,
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    },
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View the complete manifest.json source
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