SASDBS4

Glutamate decarboxylase alpha (GadA) from E. coli, low salt

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2023-06-21T07:56:39.492710+02:00

Under the experimental conditions described above, GadA exists as a mixture in solution of hexamers (volume fraction approximately 85%) and disassociated dimers (15%). The models displayed for this entry and associated fit are derived from SASREFMX modelling in P32 symmetry. The final fit to the SAXS data of the mixture was determined using OLIGOMER. The specific volume fraction estimates of the hexamer and the dimer are included in the full entry zip archive.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Glutamate decarboxylase alpha (GadA) from E. coli, low salt

Concentration— – 5.0 Buffer / pH50 mM Tris / 7.5
Experimental temperature— Facility / beamlinePETRA III / EMBL P12
Wavelength0.12 nmExposure0.05 s × 20

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Glutamate decarboxylase alpha (GadA) from E. coli
View sequence
MDQKLLTDFRSELLDSRFGAKAISTIAESKRFPLHEMRDDVAFQIINDELYLDGNARQNLATFCQTWDDENVHKLMDLSINKNWIDKEEYPQSAAIDLRCVNMVADLWHAPAPKNGQAVGTNTIGSSEACMLGGMAMKWRWRKRMEAAGKPTDKPNLVCGPVQICWHKFARYWDVELREIPMRPGQLFMDPKRMIEACDENTIGVVPTFGVTYTGNYEFPQPLHDALDKFQADTGIDIDMHIDAASGGFLAPFVAPDIVWDFRLPRVKSISASGHKFGLAPLGCGWVIWRDEEALPQELVFNVDYLGGQIGTFAINFSRPAGQVIAQYYEFLRLGREGYTKVQNASYQVAAYLADEIAKLGPYEFICTGRPDEGIPAVCFKLKDGEDPGYTLYDLSERLRLRGWQVPAFTLGGEATDIVVMRIMCRRGFEMDFAELLLEDYKASLKYLSDHPKLQGIAQQNSFKHT
proteinEscherichia coliP69908—–—monomerMolecule count 152.685 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11485[3]0.077549–4.00082 1/nmHas uncertainty columnMissing 02sasbdb/entries/s4/sasdbs4/source/SASDBS4.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
i0Guinier61228.064.0—
mwExperimental270.0—kDa
mwPorod265.0—kDa
porod_volumePorod450.0—nm³
rgGuinier4.440.01nm

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 name50 mM TrisBuffer concentration50.0 mM
pH7.5Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2015-07-29Storage / measurement temperature10.0 / —
Exposure time0.05Frames20
Wavelength0.12Sample-to-detector distance3.1
SourceX-ray synchrotronDetectorPilatus 2M
Facility / beamlinePETRA III / EMBL P12 · DESY; Hamburg, Germany
q range0.078 – 4.001Sample 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

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:172 field values
Field pathRaw value
codeSASDBS4
statusPublished
type_of_curveSingle concentration
angular_unit1/nm
project.titleX-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism.
project.publication.titleX-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism.
project.publication.author_listDadinova LA, Shtykova EV, Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
project.publication.journalPLoS One
project.publication.doi10.1371/journal.pone.0156105
project.publication.pmid27227414
project.publication.published_date2016
project.statusreleased
project.submitted_date2015-12-14
project.released_date2016-07-01
pddf_datanull
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pddf_plotnull
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experiment.instrument.detector.resolutionnull
experiment.instrument.namePETRA III
experiment.instrument.cityDESY; Hamburg
experiment.instrument.countryGermany
experiment.instrument.beamline_nameEMBL P12
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_nameGlutamate decarboxylase alpha (GadA) from E. coli
experiment.sample.molecule[0].short_nameGadA
experiment.sample.molecule[0].sequenceMDQKLLTDFRSELLDSRFGAKAISTIAESKRFPLHEMRDDVAFQIINDELYLDGNARQNL ATFCQTWDDENVHKLMDLSINKNWIDKEEYPQSAAIDLRCVNMVADLWHAPAPKNGQAVG TNTIGSSEACMLGGMAMKWRWRKRMEAAGKPTDKPNLVCGPVQICWHKFARYWDVELREI PMRPGQLFMDPKRMIEACDENTIGVVPTFGVTYTGNYEFPQPLHDALDKFQADTGIDIDM HIDAASGGFLAPFVAPDIVWDFRLPRVKSISASGHKFGLAPLGCGWVIWRDEEALPQELV FNVDYLGGQIGTFAINFSRPAGQVIAQYYEFLRLGREGYTKVQNASYQVAAYLADEIAKL GPYEFICTGRPDEGIPAVCFKLKDGEDPGYTLYDLSERLRLRGWQVPAFTLGGEATDIVV MRIMCRRGFEMDFAELLLEDYKASLKYLSDHPKLQGIAQQNSFKHT
experiment.sample.molecule[0].organismEscherichia coli
experiment.sample.molecule[0].uniprot_codeP69908
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
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experiment.sample.molecule[0].mw52.685
experiment.sample.molecule[0].total_mw52.685
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.name50 mM Tris
experiment.sample.buffer.concentration_unitmM
experiment.sample.buffer.commentnull
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experiment.sample.nameGlutamate decarboxylase alpha (GadA) from E. coli, low salt
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experiment.sample.contrastnull
experiment.sample.specific_volnull
experiment.sample.dry_volnull
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experiment.contributor[0].affiliation[0].short_nameMSU
experiment.contributor[0].affiliation[0].addressMoscow, Russia
experiment.contributor[0].affiliation[0].full_nameLomonosov Moscow State University
experiment.contributor[0].affiliation[0].webpagehttp://www.msu.ru
experiment.contributor[0].contributor_nameLiubov
experiment.contributor[0].contributor_surnameDadinova
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experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2015-07-29
experiment.storage_temperature10.0
experiment.cell_temperaturenull
experiment.exposure_time0.05
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experiment.flow_ratenull
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experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].p_value0.0
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pddf_softwarenull
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i0_calibration_standardnull
descriptionUnder the experimental conditions described above, GadA exists as a mixture in solution of hexamers (volume fraction approximately 85%) and disassociated dimers (15%). The models displayed for this entry and associated fit are derived from SASREFMX modelling in P32 symmetry. The final fit to the SAXS data of the mixture was determined using OLIGOMER. The specific volume fraction estimates of the hexamer and the dimer are included in the full entry zip archive.
experiment_descriptionSynchrotron SAXS data from solutions of Glutamate decarboxylase alpha (GadA) from E. coli in 50 mM Tris, pH 7.5 were collected on the P12 beam line of Petra-III (Hamburg, Germany) using a Pilatus 2M detector (I(s) vs s; s = 4π sin θ/λ, where 2θ is the scattering angle and λ=0.124 nm). A solute concentration of 5 mg/ml was measured using an exposure time of 1 s (recorded as 20 x 0.050 s frames). The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering from the matched solvent-blank was subtracted. The data presented here are from a single concentration scattering curve (5 mg/ml).
tags[]
intensity_unitnull
experimental_mw270.0
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guinier_i0_mwnull
guinier_i0_mw_errornull
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pddf_rg_errornull
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guinier_rg_error0.01
pddf_dmaxnull
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porod_volume_errornull
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intensities_log_log_plotSASDBS4_datloglog_img.png
symmetrynull
last_modified2023-06-21T07:56:39.492710+02:00
bragg_peak[]
manifest.json:33 field values
Field pathRaw value
codeSASDBS4
statussuccess
started_at2026-08-11T14:29:57.084946+00:00
finished_at2026-08-11T14:30:05.466887+00:00
source_last_modified2023-06-21T07:56:39.492710+02:00
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View the complete summary.json source
{
  "code": "SASDBS4",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/nm",
  "project": {
    "title": "X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism.",
    "publication": {
      "title": "X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism.",
      "author_list": "Dadinova LA, Shtykova EV, Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI",
      "journal": "PLoS One",
      "doi": "10.1371/journal.pone.0156105",
      "pmid": "27227414",
      "published_date": "2016"
    },
    "status": "released",
    "submitted_date": "2015-12-14",
    "released_date": "2016-07-01"
  },
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          "long_name": "Glutamate decarboxylase alpha (GadA) from E. coli",
          "short_name": "GadA",
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          "molecule_source": "biological",
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        }
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      "buffer": {
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        "pka": null,
        "ph": 7.5,
        "deuteration": null
      },
      "purity_method": null,
      "name": "Glutamate decarboxylase alpha (GadA) from E. coli, low salt",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
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    "contributor": [
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        "affiliation": [
          {
            "short_name": "MSU",
            "address": "Moscow, Russia",
            "full_name": "Lomonosov Moscow State University",
            "webpage": "http://www.msu.ru"
          }
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    "concentration_method": null,
    "concentration_unit": null,
    "date": "2015-07-29",
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      "software": null,
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  "description": "Under the experimental conditions described above, GadA exists as a mixture in solution of hexamers (volume fraction approximately 85%) and disassociated dimers (15%). The models displayed for this entry and associated fit are derived from SASREFMX modelling in P32 symmetry. The final fit to the SAXS data of the mixture was determined using OLIGOMER. The specific volume fraction estimates of the hexamer and the dimer are included in the full entry zip archive.",
  "experiment_description": "Synchrotron SAXS data from solutions of Glutamate decarboxylase alpha (GadA) from E. coli in 50 mM Tris, pH 7.5 were collected on the P12 beam line of Petra-III (Hamburg, Germany) using a Pilatus 2M detector (I(s) vs s; s = 4π sin θ/λ, where 2θ is the scattering angle and λ=0.124 nm). A solute concentration of 5 mg/ml was measured using an exposure time of 1 s (recorded as 20 x 0.050 s frames). The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering from the matched solvent-blank was subtracted. The data presented here are from a single concentration scattering curve (5 mg/ml). ",
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  "last_modified": "2023-06-21T07:56:39.492710+02:00",
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}
View the complete manifest.json source
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