SASDF93

Ignicoccus islandicus malate dehydrogenase

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 · Ignicoccus islandicus malate dehydrogenase

Concentration0.39 – 9.31 Buffer / pH50 mM Tris-HCl 50 mM NaCl / 7.4
Experimental temperature20.0 Facility / beamlineESRF / BM29
Wavelength0.125 nmExposure1.0 s × 10

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Malate dehydrogenase
View sequence
MARIPYKVAVIGTGRVGATFAYTMAVVPGIARMTLVDVVPGLAKGVMEDIKHAAAVFRRSITVEAFEDVSKVENADAIVITAGKPRKADMSRRDLANVNAQIIRDIGDKLRDRNPGALYVVVTNPVDVMTMVLDDVIGSKGTVIGTGTSLDTFRFRAAVSELLNVPIVAVDGYVVGEHGEEAFVAWSTVTIKGIHIDQYIKERNINISREQIEKYVKDVAASIIASQGATIWGPAATFQEIVVSHLANESKIIPISLPQNIEGVGRVAVSVPTIISGRLKPLVQLLNEEEQERLKRAAKAIRNVYESILT
proteinIgnicoccus islandicus DSM 13165A0A0U3FQH7—–—tetramerMolecule count 433.552 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11040[3]0.04474363–4.946227 1/nmHas uncertainty columnMissing 06sasbdb/entries/93/sasdf93/source/SASDF93.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)8.96—nm
i0Guinier109.120.61arbitrary
i0P(r)107.7—arbitrary
mwExperimental118.75—kDa
mwPorod124.0—kDa
porod_volumePorod198.0—nm³
rgGuinier3.260.03nm
rgP(r)3.163—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 name50 mM Tris-HCl 50 mM NaClBuffer concentration—
pH7.4Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2018-09-05Storage / measurement temperature20.0 / 20.0
Exposure time1.0Frames10
Wavelength0.125Sample-to-detector distance2.85
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineESRF / BM29 · Grenoble, France
q range0.045 – 4.946Sample 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:159 field values
Field pathRaw value
codeSASDF93
statusPublished
type_of_curveMerged
angular_unit1/nm
project.titleThe archaeal LDH-like malate dehydrogenase from Ignicoccus islandicus displays dual substrate recognition, hidden allostery and a non-canonical tetrameric oligomeric organization
project.publication.titleThe archaeal LDH-like malate dehydrogenase from Ignicoccus islandicus displays dual substrate recognition, hidden allostery and a non-canonical tetrameric oligomeric organization
project.publication.author_listRoche J, Girard E, Mas C, Madern D
project.publication.journalJournal of Structural Biology
project.publication.doi/10.1016/j.jsb.2019.07.006
project.publication.pmidnull
project.publication.published_date2019 Jul
project.statusreleased
project.submitted_date2019-02-20
project.released_date2019-07-11
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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_nameMalate dehydrogenase
experiment.sample.molecule[0].short_namenull
experiment.sample.molecule[0].sequenceMARIPYKVAVIGTGRVGATFAYTMAVVPGIARMTLVDVVPGLAKGVMEDIKHAAAVFRRSITVEAFEDVSKVENADAIVITAGKPRKADMSRRDLANVNAQIIRDIGDKLRDRNPGALYVVVTNPVDVMTMVLDDVIGSKGTVIGTGTSLDTFRFRAAVSELLNVPIVAVDGYVVGEHGEEAFVAWSTVTIKGIHIDQYIKERNINISREQIEKYVKDVAASIIASQGATIWGPAATFQEIVVSHLANESKIIPISLPQNIEGVGRVAVSVPTIISGRLKPLVQLLNEEEQERLKRAAKAIRNVYESILT
experiment.sample.molecule[0].organismIgnicoccus islandicus DSM 13165
experiment.sample.molecule[0].uniprot_codeA0A0U3FQH7
experiment.sample.molecule[0].uniprot_range_firstnull
experiment.sample.molecule[0].uniprot_range_lastnull
experiment.sample.molecule[0].oligomerizationtetramer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMARIPYKVAVIGTGRVGATFAYTMAVVPGIARMTLVDVVPGLAKGVMEDIKHAAAVFRRS ITVEAFEDVSKVENADAIVITAGKPRKADMSRRDLANVNAQIIRDIGDKLRDRNPGALYV VVTNPVDVMTMVLDDVIGSKGTVIGTGTSLDTFRFRAAVSELLNVPIVAVDGYVVGEHGE EAFVAWSTVTIKGIHIDQYIKERNINISREQIEKYVKDVAASIIASQGATIWGPAATFQE IVVSHLANESKIIPISLPQNIEGVGRVAVSVPTIISGRLKPLVQLLNEEEQERLKRAAKA IRNVYESILT
experiment.sample.molecule[0].mw33.552
experiment.sample.molecule[0].total_mw134.208
experiment.sample.molecule[0].number_molecules4
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-HCl 50 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.ph7.4
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameIgnicoccus islandicus malate dehydrogenase
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_nameIBS
experiment.contributor[0].affiliation[0].addressGrenoble, France
experiment.contributor[0].affiliation[0].full_nameInstitut de Biologie Structurale
experiment.contributor[0].affiliation[0].webpage
experiment.contributor[0].contributor_nameJennifer
experiment.contributor[0].contributor_surnameRoche
experiment.contributor[0].orcidhttps://orcid.org/0000-0002-6234-1340
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2018-09-05
experiment.storage_temperature20.0
experiment.cell_temperature20.0
experiment.exposure_time1.0
experiment.number_of_frames10
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experiment.sample_detector_distance2.85
experiment.concentration_min0.39
experiment.concentration_max9.31
experiment.sample_volumenull
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 I. islandicus malate dehydrogenase in 50 mM Tris-HCl 50 mM NaCl, pH 7.4 were collected 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 = 0.125 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.4 and 9.3 mg/ml were measured at 20°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. 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_unitarbitrary
experimental_mw118.75
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw124.0
porod_mw_errornull
pddf_i0107.7
pddf_i0_errornull
guinier_i0109.12
guinier_i0_error0.61
pddf_rg3.163
pddf_rg_errornull
guinier_rg3.26
guinier_rg_error0.03
pddf_dmax8.96
pddf_dmax_errornull
porod_volume198.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first17
guinier_point_last75
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDF93_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDF93
statussuccess
started_at2026-08-11T13:55:23.411280+00:00
finished_at2026-08-11T13:55:33.580935+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDF93",
  "status": "Published",
  "type_of_curve": "Merged",
  "angular_unit": "1/nm",
  "project": {
    "title": "The archaeal LDH-like malate dehydrogenase from Ignicoccus islandicus displays dual substrate recognition, hidden allostery and a non-canonical tetrameric oligomeric organization",
    "publication": {
      "title": "The archaeal LDH-like malate dehydrogenase from Ignicoccus islandicus displays dual substrate recognition, hidden allostery and a non-canonical tetrameric oligomeric organization",
      "author_list": "Roche J, Girard E, Mas C, Madern D",
      "journal": "Journal of Structural Biology",
      "doi": "/10.1016/j.jsb.2019.07.006",
      "pmid": null,
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    },
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      "purity_method": null,
      "name": "Ignicoccus islandicus malate dehydrogenase",
      "ext_coefficient": null,
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View the complete manifest.json source
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