SASDE99

Calredoxin with EGTA

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2019-12-17T19:23:05.803181+01:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Calredoxin with EGTA

Concentration— – 5.0 Buffer / pH20 mM Tris, 150 mM NaCl, 1 mM DTT, 5 mM EGTA / 8.0
Experimental temperature20.0 Facility / beamlineStructural Biology Laboratory, Graduate School of Medical Life Science, Yokohama City University / Rigaku BioSAXS-1000
Wavelength0.15418 nmExposure120.0 s × 2

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Calredoxin, Redox protein from Chlamydomonas reinhardtii
View sequence
MCSARSVRVVPRAATFEGLMDDASKAKMEELERRFKMADVDGNGHIDREELRNLLESMESGEVYMMSQHWLPEDELERCMEQYDVNKDGVISFEEFKQIIYDGLLLEGTLAEYESAFKAVDKSGNGTIGATELSKLFASLGNPVSLEKLVDLMQMYDKDDSGQIEFPEFLLMFRNSLLDLKDMTTYMTLDEAGAGSSGSLVDAVEGDMTLIFSEEELDALISANPDKLVVVFGALTWCRPCKGMQRPVQKLAEHYKDHIVFVKLFGNANKQTKRIFKERFQIRSTPCFITLRKGEPVYTQTGSNKEKLEAGLRSLIANPPVGMIYPSAEALAALQDPNSSSVDKLAAALEHHHHHH
proteinChlamydomonas reinhardtiiA0A2K3DZB325–357monomerMolecule count 139.901 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1974[3]0.00334162–0.668129 1/AHas uncertainty columnMissing 019sasbdb/entries/99/sasde99/source/SASDE99.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)8.67—Å
i0Guinier0.580.002arbitrary
i0P(r)0.5778—arbitrary
mwExperimental33.26—kDa
mwPorod38.0—kDa
porod_volumePorod60.0—ų
rgGuinier2.520.03Å
rgP(r)2.54—Å

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

This entry has no source fit record.

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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 name20 mM Tris, 150 mM NaCl, 1 mM DTT, 5 mM EGTABuffer concentration—
pH8.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2015-11-17Storage / measurement temperature— / 20.0
Exposure time120.0Frames2
Wavelength0.15418Sample-to-detector distance—
SourceX-ray in houseDetectorPilatus 100K
Facility / beamlineStructural Biology Laboratory, Graduate School of Medical Life Science, Yokohama City University / Rigaku BioSAXS-1000 · Yokohama, Japan
q range0.033 – 6.681Sample 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:134 field values
Field pathRaw value
codeSASDE99
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleCalcium sensing via EF-hand 4 enables thioredoxin activity in the sensor-responder protein calredoxin in the green alga <i>Chlamydomonas reinhardtii</i>.
project.publication.titleCalcium sensing via EF-hand 4 enables thioredoxin activity in the sensor-responder protein calredoxin in the green alga <i>Chlamydomonas reinhardtii</i>.
project.publication.author_listCharoenwattanasatien R, Zinzius K, Scholz M, Wicke S, Tanaka H, Brandenburg JS, Marchetti GM, Ikegami T, Matsumoto T, Oda T, Sato M, Hippler M, Kurisu G
project.publication.journalJ Biol Chem
project.publication.doi10.1074/jbc.RA119.008735
project.publication.pmid31776187
project.publication.published_date2019 Nov 27
project.statusreleased
project.submitted_date2018-12-27
project.released_date2019-12-17
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experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus 100K
experiment.instrument.detector.resolution172.0
experiment.instrument.nameStructural Biology Laboratory, Graduate School of Medical Life Science, Yokohama City University
experiment.instrument.cityYokohama
experiment.instrument.countryJapan
experiment.instrument.beamline_nameRigaku BioSAXS-1000
experiment.instrument.beam_geometrynull
experiment.instrument.type_of_sourceX-ray in house
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_nameCalredoxin, Redox protein from Chlamydomonas reinhardtii
experiment.sample.molecule[0].short_nameCRX
experiment.sample.molecule[0].sequenceMCSARSVRVVPRAATFEGLMDDASKAKMEELERRFKMADVDGNGHIDREELRNLLESMESGEVYMMSQHWLPEDELERCMEQYDVNKDGVISFEEFKQIIYDGLLLEGTLAEYESAFKAVDKSGNGTIGATELSKLFASLGNPVSLEKLVDLMQMYDKDDSGQIEFPEFLLMFRNSLLDLKDMTTYMTLDEAGAGSSGSLVDAVEGDMTLIFSEEELDALISANPDKLVVVFGALTWCRPCKGMQRPVQKLAEHYKDHIVFVKLFGNANKQTKRIFKERFQIRSTPCFITLRKGEPVYTQTGSNKEKLEAGLRSLIANPPVGMIYPSAEALAALQDPNSSSVDKLAAALEHHHHHH
experiment.sample.molecule[0].organismChlamydomonas reinhardtii
experiment.sample.molecule[0].uniprot_codeA0A2K3DZB3
experiment.sample.molecule[0].uniprot_range_first25
experiment.sample.molecule[0].uniprot_range_last357
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMIAIRTAHMLSGAQRAGSGTRVPRCSARSVRVVPRAATFEGLMDDASKAKMEELERRFKM ADVDGNGHIDREELRNLLESMESGEVYMMSQHWLPEDELERCMEQYDVNKDGVISFEEFK QIIYDGLLLEGTLAEYESAFKAVDKSGNGTIGATELSKLFASLGNPVSLEKLVDLMQMYD KDDSGQIEFPEFLLMFRNSLLDLKDMTTYMTLDEAGAGSSGSLVDAVEGDMTLIFSEEEL DALISANPDKLVVVFGALTWCRPCKGMQRPVQKLAEHYKDHIVFVKLFGNANKQTKRIFK ERFQIRSTPCFITLRKGEPVYTQTGSNKEKLEAGLRSLIANPPVGMIYPSAEALAAL
experiment.sample.molecule[0].mw39.901
experiment.sample.molecule[0].total_mw39.901
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.name20 mM Tris, 150 mM NaCl, 1 mM DTT, 5 mM EGTA
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph8.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameCalredoxin with EGTA
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].addressThailand
experiment.contributor[0].affiliation[0].full_nameSynchrotron Light Research Institute
experiment.contributor[0].affiliation[0].webpagehttps://www.slri.or.th
experiment.contributor[0].contributor_nameRatana
experiment.contributor[0].contributor_surnameCharoenwattanasatien
experiment.contributor[0].orcid
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2015-11-17
experiment.storage_temperaturenull
experiment.cell_temperature20.0
experiment.exposure_time120.0
experiment.number_of_frames2
experiment.wavelength0.15418
experiment.sample_detector_distancenull
experiment.concentration_minnull
experiment.concentration_max5.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.033
experiment.s_max6.681
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionSAXS data from solutions of Calredoxin with EGTA in 20 mM Tris, 150 mM NaCl, 1 mM DTT, 5 mM EGTA, pH 8 were collected on a Rigaku BioSAXS-1000 instrument at the Structural Biology Laboratory, Graduate School of Medical Life Science, Yokohama City University (Yokohama, Japan) using a Pilatus 100K detector at a wavelength of λ = 0.15418 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.00 mg/ml was measured at 20°C. Two successive 120 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_unitarbitrary
experimental_mw33.26
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw38.0
porod_mw_errornull
pddf_i00.5778
pddf_i0_errornull
guinier_i00.58
guinier_i0_error0.002
pddf_rg2.54
pddf_rg_errornull
guinier_rg2.52
guinier_rg_error0.03
pddf_dmax8.67
pddf_dmax_errornull
porod_volume60.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first19
guinier_point_last71
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDE99_datloglog_img.png
symmetrynull
last_modified2019-12-17T19:23:05.803181+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDE99
statussuccess
started_at2026-08-11T16:08:57.407205+00:00
finished_at2026-08-11T16:09:05.227888+00:00
source_last_modified2019-12-17T19:23:05.803181+01:00
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View the complete summary.json source
{
  "code": "SASDE99",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Calcium sensing via EF-hand 4 enables thioredoxin activity in the sensor-responder protein calredoxin in the green alga <i>Chlamydomonas reinhardtii</i>.",
    "publication": {
      "title": "Calcium sensing via EF-hand 4 enables thioredoxin activity in the sensor-responder protein calredoxin in the green alga <i>Chlamydomonas reinhardtii</i>.",
      "author_list": "Charoenwattanasatien R, Zinzius K, Scholz M, Wicke S, Tanaka H, Brandenburg JS, Marchetti GM, Ikegami T, Matsumoto T, Oda T, Sato M, Hippler M, Kurisu G",
      "journal": "J Biol Chem",
      "doi": "10.1074/jbc.RA119.008735",
      "pmid": "31776187",
      "published_date": "2019 Nov 27"
    },
    "status": "released",
    "submitted_date": "2018-12-27",
    "released_date": "2019-12-17"
  },
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          "long_name": "Calredoxin, Redox protein from Chlamydomonas reinhardtii",
          "short_name": "CRX",
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          "uniprot_range_first": 25,
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          "molecule_description": null
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  "experiment_description": "SAXS data from solutions of Calredoxin with EGTA in 20 mM Tris, 150 mM NaCl, 1 mM DTT, 5 mM EGTA, pH 8 were collected on a Rigaku BioSAXS-1000 instrument at the Structural Biology Laboratory, Graduate School of Medical Life Science, Yokohama City University (Yokohama, Japan) using a Pilatus 100K detector at a wavelength of λ = 0.15418 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.00 mg/ml was measured at 20°C. Two successive 120 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.",
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  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDE99_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2019-12-17T19:23:05.803181+01:00",
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}
View the complete manifest.json source
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