SASDCJ2

Solution structure of recombinant prion protein (89–230) in complex with Fab-P

Data type: SASBDB experimental data Status: Published Curve type: Merged Last updated: 2019-12-06T13:07:15.624532+01:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Solution structure of recombinant prion protein (89–230) in complex with Fab-P

Concentration1.0 – 3.7 Buffer / pHsodium acetate buffer (20 mM sodium acetate, pH 5.1; 150 mM NaCl) / 5.1
Experimental temperature9.8 Facility / beamlineStanford Synchrotron Radiation Lightsource (SSRL) / BL4-2
Wavelength0.113 nmExposure1.0 s × 10

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Major prion protein
View sequence
KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRS
proteinMus musculusP0492523–230monomerMolecule count 122.932 kDa
P-Clone Fab, Chimera
View sequence
ATQAYAELVMTQTPSSLSASLGERVSLTCRASQDIGNNLNWIQQKPDGTIKRLIYATSSLDSGVPKRFSGSRSGSDYSLTISSLESEDFADYYCLQHDTFPLTFGGGTKLEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRAYAEVQLLEQSGAELVKPGASVKLSCTASGFNIEDSYIHWVKQRPEQGLEWIGRIDPEDGETKYAPKFQGKATITADTSSNTAYLHLRRLTSEDTAIYYCGRGAYYIKEDFWGQGTTLTVSSASTKGPSVFPLAPSSKAGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPA
proteinHomo sapiens——–—monomerMolecule count 147.386 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1498[3]0.0124103–0.472414 1/AHas uncertainty columnMissing 00sasbdb/entries/j2/sasdcj2/source/SASDCJ2.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)14.50.5Å
i0Guinier1087.129.23—
i0P(r)1066.02.78—
mwExperimental73.8—kDa
porod_volumePorod106.0—ų
rgGuinier3.920.02Å
rgP(r)3.830.13Å

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

Fit 1 · FoXS

χ²: 1.13CorMap p: 0.058Unit: 1/A
ModelName / TypeSoftwareSymmetryModel MWPDB DeclarationSource file
1—atomicPDB (Protein Data Bank) —69.122HH0Model Image
2—atomicPDB (Protein Data Bank) —69.12—Model Image

Fit 2 · FoXS

χ²: 2.13CorMap p: 0.0Unit: 1/A
ModelName / TypeSoftwareSymmetryModel MWPDB DeclarationSource file
1—atomicPDB (Protein Data Bank) —69.12—Model Image
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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 namesodium acetate buffer (20 mM sodium acetate, pH 5.1; 150 mM NaCl)Buffer concentration—
pH5.1Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2013-12-05Storage / measurement temperature4.0 / 9.8
Exposure time1.0Frames10
Wavelength0.113Sample-to-detector distance1.7
SourceX-ray synchrotronDetectorRayonix MX225-HE
Facility / beamlineStanford Synchrotron Radiation Lightsource (SSRL) / BL4-2 · Menlo Park, CA, USA
q range0.124 – 4.724Sample 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:212 field values
Field pathRaw value
codeSASDCJ2
statusPublished
type_of_curveMerged
angular_unit1/A
project.titlePrion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering.
project.publication.titlePrion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering.
project.publication.author_listCarter L, Kim SJ, Schneidman-Duhovny D, Stöhr J, Poncet-Montange G, Weiss TM, Tsuruta H, Prusiner SB, Sali A
project.publication.journalBiophys J
project.publication.doi10.1016/j.bpj.2015.06.065
project.publication.pmid26287631
project.publication.published_date2015 Aug 18
project.statusreleased
project.submitted_date2017-04-04
project.released_date2017-06-09
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDCJ2.out
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intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDCJ2_guinier_img.png
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experiment.instrument.detector.typenull
experiment.instrument.detector.nameRayonix MX225-HE
experiment.instrument.detector.resolutionnull
experiment.instrument.nameStanford Synchrotron Radiation Lightsource (SSRL)
experiment.instrument.cityMenlo Park, CA
experiment.instrument.countryUSA
experiment.instrument.beamline_nameBL4-2
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_nameMajor prion protein
experiment.sample.molecule[0].short_nameprion
experiment.sample.molecule[0].sequenceKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWG QPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFG NDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETD VKMMERVVEQMCVTQYQKESQAYYDGRRS
experiment.sample.molecule[0].organismMus musculus
experiment.sample.molecule[0].uniprot_codeP04925
experiment.sample.molecule[0].uniprot_range_first23
experiment.sample.molecule[0].uniprot_range_last230
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMANLGYWLLALFVTMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPH GGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAV VGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVN ITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSSTVLFSSPP VILLISFLIFLIVG
experiment.sample.molecule[0].mw22.932
experiment.sample.molecule[0].total_mw22.932
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.molecule[1].long_nameP-Clone Fab, Chimera
experiment.sample.molecule[1].short_nameFab-P
experiment.sample.molecule[1].sequenceATQAYAELVMTQTPSSLSASLGERVSLTCRASQDIGNNLNWIQQKPDGTIKRLIYATSS LDSGVPKRFSGSRSGSDYSLTISSLESEDFADYYCLQHDTFPLTFGGGTKLEIKRTVAAP SVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTY SLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNR AYAEVQLLEQSGAELVKPGASVKLSCTASGFNIEDSYIHWVKQRPEQGLEWIGRIDPED GETKYAPKFQGKATITADTSSNTAYLHLRRLTSEDTAIYYCGRGAYYIKEDFWGQGTTLT VSSASTKGPSVFPLAPSSKAGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQS SGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPA
experiment.sample.molecule[1].organismHomo sapiens
experiment.sample.molecule[1].uniprot_codenull
experiment.sample.molecule[1].uniprot_range_firstnull
experiment.sample.molecule[1].uniprot_range_lastnull
experiment.sample.molecule[1].oligomerizationmonomer
experiment.sample.molecule[1].molecular_typeprotein
experiment.sample.molecule[1].uniprot_sequencenull
experiment.sample.molecule[1].mw47.386
experiment.sample.molecule[1].total_mw47.386
experiment.sample.molecule[1].number_molecules1
experiment.sample.molecule[1].complex_stateFalse
experiment.sample.molecule[1].deuterationnull
experiment.sample.molecule[1].molecule_sourcebiological
experiment.sample.molecule[1].molecule_descriptionnull
experiment.sample.buffer.namesodium acetate buffer (20 mM sodium acetate, pH 5.1; 150 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.ph5.1
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameSolution structure of recombinant prion protein (89–230) in complex with Fab-P
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_namenull
experiment.contributor[0].affiliation[0].addressJerusalem, Israel
experiment.contributor[0].affiliation[0].full_nameThe Hebrew University of Jerusalem
experiment.contributor[0].affiliation[0].webpagehttp://new.huji.ac.il
experiment.contributor[0].contributor_nameDina
experiment.contributor[0].contributor_surnameSchneidman
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2013-12-05
experiment.storage_temperature4.0
experiment.cell_temperature9.8
experiment.exposure_time1.0
experiment.number_of_frames10
experiment.wavelength0.113
experiment.sample_detector_distance1.7
experiment.concentration_min1.0
experiment.concentration_max3.7
experiment.sample_volumenull
experiment.flow_ratenull
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experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].chi_square_value1.13
fits[0].p_value0.058
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fits[1].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionGNOM V5.0 (r8972)
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from solutions of recombinant prion protein (89–230) in complex with Fab-P in 20 mM sodium acetate, 150 mM NaCl, pH 5.1 were collected on the BL4-2 beam line at the Stanford Synchrotron Radiation Lightsource (SSRL, Stanford, CA, USA) using a Rayonix MX225-HE detector at a sample-detector distance of 1.7 m and at a wavelength of λ = 0.113 nm (I(s) vs s, where s = 4πsin θ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 3.7 mg/ml were measured at 9.8°C. 10 successive 1 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 difference curves were scaled for protein concentration. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.
tags[]
intensity_unitnull
experimental_mw73.8
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i01066.0
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guinier_i01087.12
guinier_i0_error9.23
pddf_rg3.83
pddf_rg_error0.13
guinier_rg3.92
guinier_rg_error0.02
pddf_dmax14.5
pddf_dmax_error0.5
porod_volume106.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first4
guinier_point_last15
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDCJ2_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDCJ2
statussuccess
started_at2026-08-11T13:39:21.785098+00:00
finished_at2026-08-11T13:39:31.675310+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
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    "title": "Prion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering.",
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      "title": "Prion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering.",
      "author_list": "Carter L, Kim SJ, Schneidman-Duhovny D, Stöhr J, Poncet-Montange G, Weiss TM, Tsuruta H, Prusiner SB, Sali A",
      "journal": "Biophys J",
      "doi": "10.1016/j.bpj.2015.06.065",
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      "published_date": "2015 Aug 18"
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            "address": "Jerusalem, Israel",
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View the complete manifest.json source
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