SASDAB8

Protein Interacting with C-kinase 1 (PICK1) LKV, dimer contribution (data decomposition).

Data type: SASBDB experimental data Status: Published Curve type: Merged Last updated: 2023-05-25T11:22:16.556436+02:00

Structure and flexibility of PICK1 LKV mutant dimer was characterized by SAXS using data obtained by decomposing scattering from two polydisperse samples into dimer (and tetramer) contributions. To obtain the dimer scattering, two samples were measured at 4.4 and 8,8 mg/ml, and decomposed as described in the reference. Models were fitted to data using a combination of rigid body modelling and EOM, based on structural components defined by NMR and MD simulations. PDB files represent structures found in the optimal ensemble. All data, in addition to that displayed for this entry, are available in the .zip archive.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Protein Interacting with C-kinase 1 (PICK1) LKV, dimer contribution (data decomposition).

Concentration4.2 – 8.8 mg/mlBuffer / pH50 mM Tris 125 mM NaCl 0.01 vol% reduced TX-100 / 7.4
Experimental temperature4.0 Facility / beamlineDORIS III, DESY / EMBL X33
Wavelength— nmExposure40.0 s × 4

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
PRKCA-binding protein
View sequence
MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGRSIKGKTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTAELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLNKAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSGNYEYRLILRCRQEARARFSQMRKDVLEKMELLDQKHVQDIVFQLQRLVSTMSKYYNDCYAVLRDADVFPIEVDLAHTTLAYGPNQGGFTDGEDEEEEEEDGAAREVSKDARGATGPTDKGGSWLKV
proteinRattus norvegicusQ9EP802–416dimerMolecule count 246.506 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1116[4]0.0675000018–6.26464963 1/nmHas uncertainty columnMissing 00sasbdb/entries/b8/sasdab8/source/SASDAB8.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)20.0—nm
i0Guinier1.070.01—
i0P(r)1.0290.01—
mwExperimental92.0—kDa
mwGuinier I(0)92.0—kDa
porod_volumePorod205.0—nm³
rgGuinier6.0170.91nm
rgP(r)6.030.05nm

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 name50 mM Tris 125 mM NaCl 0.01 vol% reduced TX-100Buffer concentration50.0 mM
pH7.4Additives125 mM NaCl, 0.01 vol% reduced TX-100
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2015-05-11Storage / measurement temperature— / 4.0
Exposure time40.0Frames4
Wavelength—Sample-to-detector distance—
SourceX-ray synchrotronDetectorMAR 345 Image Plate
Facility / beamlineDORIS III, DESY / EMBL X33 · Hamburg, Germany
q range0.068 – 6.265Sample 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
codeSASDAB8
statusPublished
type_of_curveMerged
angular_unit1/nm
project.titleStructure of Dimeric and Tetrameric Complexes of the BAR Domain Protein PICK1 Determined by Small-Angle X-Ray Scattering.
project.publication.titleStructure of Dimeric and Tetrameric Complexes of the BAR Domain Protein PICK1 Determined by Small-Angle X-Ray Scattering.
project.publication.author_listKarlsen ML, Thorsen TS, Johner N, Ammendrup-Johnsen I, Erlendsson S, Tian X, Simonsen JB, Høiberg-Nielsen R, Christensen NM, Khelashvili G, Streicher W, Teilum K, Vestergaard B, Weinstein H, Gether U, Arleth L, Madsen KL
project.publication.journalStructure
project.publication.doi10.1016/j.str.2015.04.020
project.publication.pmid26073603
project.publication.published_date2015 Jul 7
project.statusreleased
project.submitted_date2015-05-10
project.released_date2015-07-07
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experiment.instrument.detector.resolutionnull
experiment.instrument.nameDORIS III, DESY
experiment.instrument.cityHamburg
experiment.instrument.countryGermany
experiment.instrument.beamline_nameEMBL X33
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
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experiment.instrument.xray_energynull
experiment.instrument.beam_profile_ahnull
experiment.instrument.beam_profile_alnull
experiment.sample.molecule[0].long_namePRKCA-binding protein
experiment.sample.molecule[0].short_namenull
experiment.sample.molecule[0].sequenceMFADLDYDIEEDKLGI PTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGR SIKGKTKVEVAKMIQEVKGEVTIHYNK LQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAIL CNDGLVKRLEELERTAELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAAS EAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLNKAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSGNYEYRLILRCRQEARARFSQMRKDVLEKMELLDQKHVQDIVFQLQRLVSTMSKYYNDCYAVLRDADVFPIEVDLAHTTLAYGPNQGGFTDGEDEEEEEEDGAAREVSKDARGATGPTDKGGSWLKV
experiment.sample.molecule[0].organismRattus norvegicus
experiment.sample.molecule[0].uniprot_codeQ9EP80
experiment.sample.molecule[0].uniprot_range_first2
experiment.sample.molecule[0].uniprot_range_last416
experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAAL DGTVAAGDEITGVNGRSIKGKTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKK VKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTAELYKGMTEHTKNLLRAFYEL SQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLN KAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSTGNYEYRLILRC RQEARARFSQMRKDVLEKMELLDQKHVQDIVFQLQRFVSTMSKYYNDCYAVLRDADVFPI EVDLAHTTLAYGPNQGGFTDGEDEEEEEEDGAAREVSKDARGATGPTDKGGSWCDS
experiment.sample.molecule[0].mw46.506
experiment.sample.molecule[0].total_mw93.011
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.name50 mM Tris 125 mM NaCl 0.01 vol% reduced TX-100
experiment.sample.buffer.concentration_unitmM
experiment.sample.buffer.commentnull
experiment.sample.buffer.additive125 mM NaCl, 0.01 vol% reduced TX-100
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experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.4
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experiment.sample.nameProtein Interacting with C-kinase 1 (PICK1) LKV, dimer contribution (data decomposition).
experiment.sample.ext_coefficientnull
experiment.sample.contrastnull
experiment.sample.specific_volnull
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experiment.sample.mixturenull
experiment.contributor[0].affiliation[0].short_namenull
experiment.contributor[0].affiliation[0].addressCopenhagen, Denmark
experiment.contributor[0].affiliation[0].full_nameUniversity of Copenhagen
experiment.contributor[0].affiliation[0].webpagehttp://www.ku.dk/
experiment.contributor[0].contributor_nameMorten
experiment.contributor[0].contributor_surnameKarlsen
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitmg/ml
experiment.date2015-05-11
experiment.storage_temperaturenull
experiment.cell_temperature4.0
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i0_calibration_standardBSA
descriptionStructure and flexibility of PICK1 LKV mutant dimer was characterized by SAXS using data obtained by decomposing scattering from two polydisperse samples into dimer (and tetramer) contributions. To obtain the dimer scattering, two samples were measured at 4.4 and 8,8 mg/ml, and decomposed as described in the reference. Models were fitted to data using a combination of rigid body modelling and EOM, based on structural components defined by NMR and MD simulations. PDB files represent structures found in the optimal ensemble. All data, in addition to that displayed for this entry, are available in the .zip archive.
experiment_descriptionnull
tags[0]X33
intensity_unitnull
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guinier_point_last34
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symmetrynull
last_modified2023-05-25T11:22:16.556436+02:00
bragg_peak[]
manifest.json:36 field values
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codeSASDAB8
statussuccess
started_at2026-08-11T15:49:33.173709+00:00
finished_at2026-08-11T15:49:44.084007+00:00
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View the complete summary.json source
{
  "code": "SASDAB8",
  "status": "Published",
  "type_of_curve": "Merged",
  "angular_unit": "1/nm",
  "project": {
    "title": "Structure of Dimeric and Tetrameric Complexes of the BAR Domain Protein PICK1 Determined by Small-Angle X-Ray Scattering.",
    "publication": {
      "title": "Structure of Dimeric and Tetrameric Complexes of the BAR Domain Protein PICK1 Determined by Small-Angle X-Ray Scattering.",
      "author_list": "Karlsen ML, Thorsen TS, Johner N, Ammendrup-Johnsen I, Erlendsson S, Tian X, Simonsen JB, Høiberg-Nielsen R, Christensen NM, Khelashvili G, Streicher W, Teilum K, Vestergaard B, Weinstein H, Gether U, Arleth L, Madsen KL",
      "journal": "Structure",
      "doi": "10.1016/j.str.2015.04.020",
      "pmid": "26073603",
      "published_date": "2015 Jul 7"
    },
    "status": "released",
    "submitted_date": "2015-05-10",
    "released_date": "2015-07-07"
  },
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View the complete manifest.json source
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