SASDDZ5

AMPA subtype ionotropic Glutamate receptor GluA2 in the AMPA bound state, in stealth DDM detergents, pH 7.5

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2019-12-06T13:07:15.624532+01:00

Sample of GluA2 in the AMPA bound state at neutral pH. The SANS data were fitted with a mixture of GluA2 in a tetrameric compact form and a fraction of oligimers of the compact tetramer. Three models fitted equally well (within a 5% significance level): a mixture of GluA2 in the activated state (pdb-code 5weo) and a fraction of oligomers (top fit: fit62.dat), a mixture of GluA2 in the desensitized state (pdb-code 5vhz) and a fraction of oligomers (middle fit: fit63.dat) and a mixture of GluA2 in the resting state (pdb-code 4u2p) and a fraction of oligomers (bottom fit: fit72.dat). The oligomers were described with a fractal structure factor (Teixeira, J. (1988). J. Appl. Crystallogr. 21, 781-785). Data were fitted with WillItFit (Pedersen, M. C., Arleth, L. & Mortensen, K. (2013). J. Appl. Crystallogr. 46, 1894-1898). The SANS data were measured in three settings (sample/collimation): 1.5m/4.m, 4m/4m, and 8m/8m. The attached data are merged into one data set with all three settings. Pair distance distribution functions were calculated with BayesApp (www.bayesapp.org). Due to relatively low protein concentration, the concentration measurement was inaccurate, and the MW was therefore evaluated by (concentration independent) Porod analysis using the Porod volume calculator implemented in PRIMUS, and with a volume-to-mass conversion constant of 0.83 kDa/nm^3 (Gekko, K. & Noguchi, H. (1979). J. Phys. Chem. 83, 2706-2714; Squire, P. G. & Himmel, M. E. (1979). Arch. Biochem. Biophys. 196, 165-177).

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · AMPA subtype ionotropic Glutamate receptor GluA2 in the AMPA bound state, in stealth DDM detergents, pH 7.5

Concentration— – 0.31 Buffer / pHD2O based buffer. 1 mM AMPA, 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O) / 7.5
Experimental temperature10.0 Facility / beamlineFRM2 / KWS1
Wavelength0.5 nmExposure900.0 s × 15

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Glutamate receptor 2
View sequence
NSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVLTEDDTSGLEQKTVVVTTILESPYVMMKANHAALAGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMQQGADISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGTPVNLAVLKLSEQGLLDKLKNKWWYDKGECGAKDSGSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKGLVPRGNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVLTEDDTSGLEQKTVVVTTILESPYVMMKANHAALAGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMQQGADISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGTPVNLAVLKLSEQGLLDKLKNKWWYDKGECGAKDSGSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKGLVPRGNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVLTEDDTSGLEQKTVVVTTILESPYVMMKANHAALAGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMQQGADISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGTPVNLAVLKLSEQGLLDKLKNKWWYDKGECGAKDSGSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKGLVPRGNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVLTEDDTSGLEQKTVVVTTILESPYVMMKANHAALAGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMQQGADISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGTPVNLAVLKLSEQGLLDKLKNKWWYDKGECGAKDSGSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKGLVPRG
proteinRattus norvegicusP19491—–—monomerMolecule count 1367.694 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1115[4]0.006897303–0.1985586 1/AHas uncertainty columnMissing 00sasbdb/entries/z5/sasddz5/source/SASDDZ5.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)18.41.1Å
i0Guinier0.110.0011/cm
i0P(r)0.1060.0007911/cm
mwExperimental338.0—kDa
mwPorod338.0—kDa
porod_volumePorod407.0—ų
rgGuinier6.250.06Å
rgP(r)6.10.06Å

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 nameD2O based buffer. 1 mM AMPA, 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O)Buffer concentration—
pH7.5Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2016-10-19Storage / measurement temperature10.0 / 10.0
Exposure time900.0Frames15
Wavelength0.5Sample-to-detector distance—
Sourceneutron sourceDetector6Li-Scintillator 1 mm thickness + photomultiplier
Facility / beamlineFRM2 / KWS1 · Munich, Germany
q range0.069 – 1.986Sample 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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full_entry_zip:source record and ZIP contents (5 items)
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sascif:source record
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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:166 field values
Field pathRaw value
codeSASDDZ5
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleSmall-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states.
project.publication.titleSmall-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states.
project.publication.author_listLarsen AH, Dorosz J, Thorsen TS, Johansen NT, Darwish T, Midtgaard SR, Arleth L, Kastrup JS
project.publication.journalIUCrJ
project.publication.doi10.1107/S2052252518012186
project.publication.pmid30443361
project.publication.published_date2018 Nov 1
project.statusreleased
project.submitted_date2018-04-10
project.released_date2018-10-10
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDDZ5_pr.dat
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDDZ5.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDDZ5_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDDZ5_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDDZ5_pr_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDDZ5_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDDZ5.sascif
experiment.instrument.detector.typeSANS
experiment.instrument.detector.name6Li-Scintillator 1 mm thickness + photomultiplier
experiment.instrument.detector.resolution5.3
experiment.instrument.nameFRM2
experiment.instrument.cityMunich
experiment.instrument.countryGermany
experiment.instrument.beamline_nameKWS1
experiment.instrument.beam_geometrynull
experiment.instrument.type_of_sourceneutron source
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_nameGlutamate receptor 2
experiment.sample.molecule[0].short_nameGluA2
experiment.sample.molecule[0].sequenceNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFC GTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNIN NDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVD YDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEI ERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVLTEDDTSGLEQKTVVVTTILESPYVMMK ANHAALAGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVI DFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTN EFGIFNSLWFSLGAFMQQGADISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGT LDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDS KGYGIATPKGSSLGTPVNLAVLKLSEQGLLDKLKNKWWYDKGECGAKDSGSKEKTSALSLSNVAGVFYILVGGLGLAMLV ALIEFCYKSRAEAKRMKGLVPRG NSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFC GTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNIN NDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVD YDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEI ERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVLTEDDTSGLEQKTVVVTTILESPYVMMK ANHAALAGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVI DFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTN EFGIFNSLWFSLGAFMQQGADISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGT LDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDS KGYGIATPKGSSLGTPVNLAVLKLSEQGLLDKLKNKWWYDKGECGAKDSGSKEKTSALSLSNVAGVFYILVGGLGLAMLV ALIEFCYKSRAEAKRMKGLVPRG NSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFC GTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNIN NDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVD YDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEI ERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVLTEDDTSGLEQKTVVVTTILESPYVMMK ANHAALAGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVI DFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTN EFGIFNSLWFSLGAFMQQGADISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGT LDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDS KGYGIATPKGSSLGTPVNLAVLKLSEQGLLDKLKNKWWYDKGECGAKDSGSKEKTSALSLSNVAGVFYILVGGLGLAMLV ALIEFCYKSRAEAKRMKGLVPRG NSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFC GTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNIN NDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGAEVSGFQIVD YDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEI ERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVLTEDDTSGLEQKTVVVTTILESPYVMMK ANHAALAGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVI DFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTN EFGIFNSLWFSLGAFMQQGADISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGT LDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDS KGYGIATPKGSSLGTPVNLAVLKLSEQGLLDKLKNKWWYDKGECGAKDSGSKEKTSALSLSNVAGVFYILVGGLGLAMLV ALIEFCYKSRAEAKRMKGLVPRG
experiment.sample.molecule[0].organismRattus norvegicus
experiment.sample.molecule[0].uniprot_codeP19491
experiment.sample.molecule[0].uniprot_range_firstnull
experiment.sample.molecule[0].uniprot_range_lastnull
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTP HIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDG THPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINV GNINNDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANL GFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALT YDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNI KFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTT ILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKI WNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLD PLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWF SLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDL SKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGK YAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLKLNEQGLL DKLKNKWWYDKGECGSGGGDSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSR AEAKRMKVAKNPQNINPSSSQNSQNFATYKEGYNVYGIESVKI
experiment.sample.molecule[0].mw367.694
experiment.sample.molecule[0].total_mw367.694
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.nameD2O based buffer. 1 mM AMPA, 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O)
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameAMPA subtype ionotropic Glutamate receptor GluA2 in the AMPA bound state, in stealth DDM detergents, pH 7.5
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].addressCopenhagen, Denmark
experiment.contributor[0].affiliation[0].full_nameUniversity of Copenhagen
experiment.contributor[0].affiliation[0].webpagehttp://www.ku.dk/
experiment.contributor[0].contributor_nameAndreas
experiment.contributor[0].contributor_surnameLarsen
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2016-10-19
experiment.storage_temperature10.0
experiment.cell_temperature10.0
experiment.exposure_time900.0
experiment.number_of_frames15
experiment.wavelength0.5
experiment.sample_detector_distancenull
experiment.concentration_minnull
experiment.concentration_max0.31
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.069
experiment.s_max1.986
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[0].models[]
fits[0].fit_unit1/A
fits[0].fit_plothttps://www.sasbdb.org/media/fitting_files/scattering_plots/SASDDZ5_fit1_fitfoxs_img.png
fits[0].softwareOther
fits[0].chi_square_value5.0
fits[0].p_value0.0
fits[0].fit_residual_plotSASDDZ5_fit1_fitfoxsresiduals_img.png
fits[0].fit_datahttps://www.sasbdb.org/media/fitting_files/SASDDZ5_fit1.dat
fits[0].fit_lognull
fits[0].software_versionWillItFit
fits[0].descriptionnull
fits[1].models[]
fits[1].fit_unit1/A
fits[1].fit_plothttps://www.sasbdb.org/media/fitting_files/scattering_plots/SASDDZ5_fit2_fitfoxs_img.png
fits[1].softwareOther
fits[1].chi_square_value5.8
fits[1].p_value0.0
fits[1].fit_residual_plotSASDDZ5_fit2_fitfoxsresiduals_img.png
fits[1].fit_datahttps://www.sasbdb.org/media/fitting_files/SASDDZ5_fit2.dat
fits[1].fit_lognull
fits[1].software_versionWillItFit
fits[1].descriptionnull
fits[2].models[]
fits[2].fit_unit1/A
fits[2].fit_plothttps://www.sasbdb.org/media/fitting_files/scattering_plots/SASDDZ5_fit3_fitfoxs_img.png
fits[2].softwareOther
fits[2].chi_square_value5.9
fits[2].p_value0.0
fits[2].fit_residual_plotSASDDZ5_fit3_fitfoxsresiduals_img.png
fits[2].fit_datahttps://www.sasbdb.org/media/fitting_files/SASDDZ5_fit3.dat
fits[2].fit_lognull
fits[2].software_versionWillItFit
fits[2].descriptionnull
estimated_volume_methodnull
pddf_softwareCustom in-house
pddf_software_versionBayesApp
i0_calibration_standardnull
descriptionSample of GluA2 in the AMPA bound state at neutral pH. The SANS data were fitted with a mixture of GluA2 in a tetrameric compact form and a fraction of oligimers of the compact tetramer. Three models fitted equally well (within a 5% significance level): a mixture of GluA2 in the activated state (pdb-code 5weo) and a fraction of oligomers (top fit: fit62.dat), a mixture of GluA2 in the desensitized state (pdb-code 5vhz) and a fraction of oligomers (middle fit: fit63.dat) and a mixture of GluA2 in the resting state (pdb-code 4u2p) and a fraction of oligomers (bottom fit: fit72.dat). The oligomers were described with a fractal structure factor (Teixeira, J. (1988). J. Appl. Crystallogr. 21, 781-785). Data were fitted with WillItFit (Pedersen, M. C., Arleth, L. & Mortensen, K. (2013). J. Appl. Crystallogr. 46, 1894-1898). The SANS data were measured in three settings (sample/collimation): 1.5m/4.m, 4m/4m, and 8m/8m. The attached data are merged into one data set with all three settings. Pair distance distribution functions were calculated with BayesApp (www.bayesapp.org). Due to relatively low protein concentration, the concentration measurement was inaccurate, and the MW was therefore evaluated by (concentration independent) Porod analysis using the Porod volume calculator implemented in PRIMUS, and with a volume-to-mass conversion constant of 0.83 kDa/nm^3 (Gekko, K. & Noguchi, H. (1979). J. Phys. Chem. 83, 2706-2714; Squire, P. G. & Himmel, M. E. (1979). Arch. Biochem. Biophys. 196, 165-177).
experiment_descriptionSANS data from solutions of Glutamate receptor 2 (GluA2) in the AMPA bound state, at neutral pH in D2O based buffer. 1 mM AMPA, 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O), pH 7.5 were collected on the KWS1 camera at the FRM2 storage ring (Munich, Germany) using a 6Li-Scintillator 1 mm thickness + photomultiplier detector at a wavelength of λ = 0.5 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 0.31 mg/ml was measured at 10°C. 15 successive 900 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.
tags[]
intensity_unit1/cm
experimental_mw338.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw338.0
porod_mw_errornull
pddf_i00.106
pddf_i0_error0.000791
guinier_i00.11
guinier_i0_error0.001
pddf_rg6.1
pddf_rg_error0.06
guinier_rg6.25
guinier_rg_error0.06
pddf_dmax18.4
pddf_dmax_error1.1
porod_volume407.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first1
guinier_point_last23
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDDZ5_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDDZ5
statussuccess
started_at2026-08-11T14:59:33.749958+00:00
finished_at2026-08-11T14:59:40.497092+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDDZ5",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Small-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states.",
    "publication": {
      "title": "Small-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states.",
      "author_list": "Larsen AH, Dorosz J, Thorsen TS, Johansen NT, Darwish T, Midtgaard SR, Arleth L, Kastrup JS",
      "journal": "IUCrJ",
      "doi": "10.1107/S2052252518012186",
      "pmid": "30443361",
      "published_date": "2018 Nov 1"
    },
    "status": "released",
    "submitted_date": "2018-04-10",
    "released_date": "2018-10-10"
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      "beam_profile_ah": null,
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        "affiliation": [
          {
            "short_name": null,
            "address": "Copenhagen, Denmark",
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          }
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    "concentration_unit": null,
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    "seccolumn": null
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      "fit_log": null,
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  "description": "Sample of GluA2 in the AMPA bound state at neutral pH. The SANS data were fitted with a mixture of GluA2 in a tetrameric compact form and a fraction of oligimers of the compact tetramer. Three models fitted equally well (within a 5% significance level): a mixture of GluA2 in the activated state (pdb-code 5weo) and a fraction of oligomers (top fit: fit62.dat), a mixture of GluA2 in the desensitized state (pdb-code 5vhz) and a fraction of oligomers (middle fit: fit63.dat) and a mixture of GluA2 in the resting state (pdb-code 4u2p) and a fraction of oligomers (bottom fit: fit72.dat). The oligomers were described with a fractal structure factor (Teixeira, J. (1988). J. Appl. Crystallogr. 21, 781-785). Data were fitted with WillItFit (Pedersen, M. C., Arleth, L. & Mortensen, K. (2013). J. Appl. Crystallogr. 46, 1894-1898). The SANS data were measured in three settings (sample/collimation): 1.5m/4.m, 4m/4m, and 8m/8m. The attached data are merged into one data set with all three settings. Pair distance distribution functions were calculated with BayesApp (www.bayesapp.org). Due to relatively low protein concentration, the concentration measurement was inaccurate, and the MW was therefore evaluated by (concentration independent) Porod analysis using the Porod volume calculator implemented in PRIMUS, and with a volume-to-mass conversion constant of 0.83 kDa/nm^3 (Gekko, K. & Noguchi, H. (1979). J. Phys. Chem. 83, 2706-2714; Squire, P. G. & Himmel, M. E. (1979). Arch. Biochem. Biophys. 196, 165-177).",
  "experiment_description": "SANS data from solutions of Glutamate receptor 2 (GluA2) in the AMPA bound state, at neutral pH in D2O based buffer. 1 mM AMPA, 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O), pH 7.5 were collected on the KWS1 camera at the FRM2 storage ring (Munich, Germany) using a 6Li-Scintillator 1 mm thickness + photomultiplier detector at a wavelength of λ = 0.5 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 0.31 mg/ml was measured at 10°C. 15 successive 900 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.",
  "tags": [],
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  "estimated_volume": null,
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  "guinier_point_first": 1,
  "guinier_point_last": 23,
  "pddf_point_first": null,
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  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDDZ5_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2019-12-06T13:07:15.624532+01:00",
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}
View the complete manifest.json source
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