SASDD47

The ferredoxin protease, FusC, E83A mutant + 100 µM Arabidopsis ferredoxin

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

The FusC E83A mutant (30 µM) in the presence of 100 µM Arabidopsis ferredoxin. The background subtraction included 100 µM Arabidopsis ferredoxin in buffer.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · The ferredoxin protease, FusC, E83A mutant + 100 µM Arabidopsis ferredoxin

Concentration— – 3.0 Buffer / pH20 mM Tris, 150 mM NaCl / 7.8
Experimental temperature20.0 Facility / beamlineAustralian Synchrotron / SAXS/WAXS
Wavelength0.103 nmExposure— s × —

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Ferredoxin protease E83A mutant
View sequence
EEIKSPLPVFKEGTLANGFRYTLVQLEGPKTRVDIRLIVDVGSIDEKDNESGVAHMVAHMVFRASDAFPQGVSTELHKQGWGRGQSYNAVTNYERTMYMMSPPKGNLDLGATLQALSQMTGHAKLLQSDLDDERKIILEEWRGKLGVAERMNQQRVQAIRHDSRYPSRPVIGTEESINDTPASVLQDFYQRWYHPSNMRLMIIGDITPADAEREIQRYFAALPNVAVPTRDYYEPLLKPQLKVARLQDSQSGSSQVSFVYRFNDKDAFGQSEYRHRLLTQITMSAVTRQVRRQKAELPQDASSLVVRKSDIGKTTAALGFFANVMPGGHDAAISAVLKEIERFKRYPLNEQDITEITSDIREVAQRMSVTPETREFADWVQQLTIVWQQDRPYVGSQQRGKDALEALDTIKGEDVNRHWQRWLASPDTLAQFSVPGATPFTLPKPDAISKLQKQWALATLAPLRLEEKKIIPELPSVTQSGKRTAVKTFAAQKVEQWQLSNGDRVVWLRAPEAGKKVYLTATSQAGFMATAMNPWQAQLASQLVNQSGPATWSGESLSNWKKEKTLSLSIDQEADQLTLSGTAPTEQLASLFGLYRELNVAPGIDPDVMKESMMSLARQKANDDQSVGGKRASEMTKLRFGEPAWQQPEIAELKKISAPALLSQWHKAASAPVTYYLIADMPATQLLPQVERYLATIPRQPASEVKQHLALSGKREATSAINVEPRADILTWSFTPHAWTPQAAVQVSIARNIASKYLKTSLRDDALGIYRMRVDSELEDKKQRIETEVSFTSAPERAQELWTLAEQAFSELPTKITQQDVDEQKAQFIRAEKGRQGDLTTIQRRLILSYRHYNDPRYLSNASKLADSITLESVRAMSAKLYNPDNRVLYITLPQEVKE
proteinPectobacterium atrosepticum SCRI1043Q6D8U326–924monomerMolecule count 1101.195 kDa
Arabidopsis ferredoxin 2
View sequence
ATYKVKFITPEGELEVECDDDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSVDQSDQSFLDDEQIGEGFVLTCAAYPTSDVTIETHKEEAIMLEHHHHHH
proteinArabidopsis thalianaP1697253–145monomerMolecule count 111.33 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1400[3]0.0113693–0.303754 1/AHas uncertainty columnMissing 00sasbdb/entries/47/sasdd47/source/SASDD47.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)13.69—Å
i0Guinier0.280.00032arbitrary
i0P(r)0.2708—arbitrary
mwExperimental100.0—kDa
mwPorod103.9—kDa
porod_volumePorod176.7—ų
rgGuinier3.720.064Å
rgP(r)3.81—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 NaClBuffer concentration—
pH7.8Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2017-10-26Storage / measurement temperature20.0 / 20.0
Exposure time—Frames—
Wavelength0.103Sample-to-detector distance1.28
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineAustralian Synchrotron / SAXS/WAXS · Melbourne, Australia
q range0.114 – 3.038Sample 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

CategoryFileStatusSizeChecksumDownload and View
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full_entry_zip:source record and ZIP contents (2 items)
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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:151 field values
Field pathRaw value
codeSASDD47
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleFusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants.
project.publication.titleFusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants.
project.publication.author_listGrinter R, Hay ID, Song J, Wang J, Teng D, Dhanesakaran V, Wilksch JJ, Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T
project.publication.journalPLoS Biol
project.publication.doi10.1371/journal.pbio.2006026
project.publication.pmid30071011
project.publication.published_date2018 Aug
project.statusreleased
project.submitted_date2018-05-19
project.released_date2018-06-13
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDD47.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDD47.dat
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pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDD47_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDD47_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDD47.sascif
experiment.instrument.detector.typeDectris
experiment.instrument.detector.namePilatus 1M
experiment.instrument.detector.resolution172.0
experiment.instrument.nameAustralian Synchrotron
experiment.instrument.cityMelbourne
experiment.instrument.countryAustralia
experiment.instrument.beamline_nameSAXS/WAXS
experiment.instrument.beam_geometryPoint
experiment.instrument.type_of_sourceX-ray synchrotron
experiment.instrument.point_sourceTrue
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_nameFerredoxin protease E83A mutant
experiment.sample.molecule[0].short_nameFusC E83A
experiment.sample.molecule[0].sequenceEEIKSPLPVFKEGTLANGFRYTLVQLEGPKTRVDIRLIVDVGSIDEKDNESGVAH MVAHMVFRASDAFPQGVSTELHKQGWGRGQSYNAVTNYERTMYMMSPPKGNLDLGATLQALSQMTGHAKLLQSDLDDERK IILEEWRGKLGVAERMNQQRVQAIRHDSRYPSRPVIGTEESINDTPASVLQDFYQRWYHPSNMRLMIIGDITPADAEREI QRYFAALPNVAVPTRDYYEPLLKPQLKVARLQDSQSGSSQVSFVYRFNDKDAFGQSEYRHRLLTQITMSAVTRQVRRQKA ELPQDASSLVVRKSDIGKTTAALGFFANVMPGGHDAAISAVLKEIERFKRYPLNEQDITEITSDIREVAQRMSVTPETRE FADWVQQLTIVWQQDRPYVGSQQRGKDALEALDTIKGEDVNRHWQRWLASPDTLAQFSVPGATPFTLPKPDAISKLQKQW ALATLAPLRLEEKKIIPELPSVTQSGKRTAVKTFAAQKVEQWQLSNGDRVVWLRAPEAGKKVYLTATSQAGFMATAMNPW QAQLASQLVNQSGPATWSGESLSNWKKEKTLSLSIDQEADQLTLSGTAPTEQLASLFGLYRELNVAPGIDPDVMKESMMS LARQKANDDQSVGGKRASEMTKLRFGEPAWQQPEIAELKKISAPALLSQWHKAASAPVTYYLIADMPATQLLPQVERYLA TIPRQPASEVKQHLALSGKREATSAINVEPRADILTWSFTPHAWTPQAAVQVSIARNIASKYLKTSLRDDALGIYRMRVD SELEDKKQRIETEVSFTSAPERAQELWTLAEQAFSELPTKITQQDVDEQKAQFIRAEKGRQGDLTTIQRRLILSYRHYND PRYLSNASKLADSITLESVRAMSAKLYNPDNRVLYITLPQEVKE
experiment.sample.molecule[0].organismPectobacterium atrosepticum SCRI1043
experiment.sample.molecule[0].uniprot_codeQ6D8U3
experiment.sample.molecule[0].uniprot_range_first26
experiment.sample.molecule[0].uniprot_range_last924
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMNWKKCCWLSLTAVGLLAGSVVSQAEEIKSPLPVFKEGTLANGFRYTLVQLEGPKTRVDI RLIVDVGSIDEKDNESGVAHMVEHMVFRASDAFPQGVSTELHKQGWGRGQSYNAVTNYER TMYMMSPPKGNLDLGATLQALSQMTGHAKLLQSDLDDERKIILEEWRGKLGVAERMNQQR VQAIRHDSRYPSRPVIGTEESINDTPASVLQDFYQRWYHPSNMRLMIIGDITPADAEREI QRYFAALPNVAVPTRDYYEPLLKPQLKVARLQDSQSGSSQVSFVYRFNDKDAFGQSEYRH RLLTQITMSAVTRQVRRQKAELPQDASSLVVRKSDIGKTTAALGFFANVMPGGHDAAISA VLKEIERFKRYPLNEQDITEITSDIREVAQRMSVTPETREFADWVQQLTIVWQQDRPYVG SQQRGKDALEALDTIKGEDVNRHWQRWLASPDTLAQFSVPGATPFTLPKPDAISKLQKQW ALATLAPLRLEEKKIIPELPSVTQSGKRTAVKTFAAQKVEQWQLSNGDRVVWLRAPEAGK KVYLTATSQAGFMATAMNPWQAQLASQLVNQSGPATWSGESLSNWKKEKTLSLSIDQEAD QLTLSGTAPTEQLASLFGLYRELNVAPGIDPDVMKESMMSLARQKANDDQSVGGKRASEM TKLRFGEPAWQQPEIAELKKISAPALLSQWHKAASAPVTYYLIADMPATQLLPQVERYLA TIPRQPASEVKQHLALSGKREATSAINVEPRADILTWSFTPHAWTPQAAVQVSIARNIAS KYLKTSLRDDALGIYRMRVDSELEDKKQRIETEVSFTSAPERAQELWTLAEQAFSELPTK ITQQDVDEQKAQFIRAEKGRQGDLTTIQRRLILSYRHYNDPRYLSNASKLADSITLESVR AMSAKLYNPDNRVLYITLPQEVKE
experiment.sample.molecule[0].mw101.195
experiment.sample.molecule[0].total_mw101.195
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_nameArabidopsis ferredoxin 2
experiment.sample.molecule[1].short_nameAra_Fer2
experiment.sample.molecule[1].sequenceATYKVKFITPEGELEVECDDDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSVDQSDQSFLDDEQIGEGFVLTCAAYPTSDVTIETHKEEAIMLEHHHHHH
experiment.sample.molecule[1].organismArabidopsis thaliana
experiment.sample.molecule[1].uniprot_codeP16972
experiment.sample.molecule[1].uniprot_range_first53
experiment.sample.molecule[1].uniprot_range_last145
experiment.sample.molecule[1].oligomerizationmonomer
experiment.sample.molecule[1].molecular_typeprotein
experiment.sample.molecule[1].uniprot_sequenceMASTALSSAIVGTSFIRRSPAPISLRSLPSANTQSLFGLKSGTARGGRVTAMATYKVKFI TPEGELEVECDDDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSVDQSDQSFLDDEQ IGEGFVLTCAAYPTSDVTIETHKEEDIV
experiment.sample.molecule[1].mw11.33
experiment.sample.molecule[1].total_mw11.33
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.name20 mM Tris, 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.ph7.8
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameThe ferredoxin protease, FusC, E83A mutant + 100 µM Arabidopsis ferredoxin
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].addressMelbourne, Australia
experiment.contributor[0].affiliation[0].full_nameMonash University
experiment.contributor[0].affiliation[0].webpagehttp://www.monash.edu/
experiment.contributor[0].contributor_nameGrinter
experiment.contributor[0].contributor_surnameGrinter
experiment.contributor[0].orcidhttps://orcid.org/0000-0002-8195-5348
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2017-10-26
experiment.storage_temperature20.0
experiment.cell_temperature20.0
experiment.exposure_timenull
experiment.number_of_framesnull
experiment.wavelength0.103
experiment.sample_detector_distance1.28
experiment.concentration_minnull
experiment.concentration_max3.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.114
experiment.s_max3.038
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionThe FusC E83A mutant (30 µM) in the presence of 100 µM Arabidopsis ferredoxin. The background subtraction included 100 µM Arabidopsis ferredoxin in buffer.
experiment_descriptionSynchrotron SAXS data from solutions of ferredoxin protease, FusC, E83A mutant + 100 µM Arabidopsis ferredoxin in 20 mM Tris, 150 mM NaCl, pH 7.8 were collected on the SAXS/WAXS beam line at the Australian Synchrotron storage ring (Melbourne, Australia) using a Pilatus 1M detector at a sample-detector distance of 1.3 m and at a wavelength of λ = 0.103 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.00 mg/ml was measured at 20°C. 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_mw100.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw103.9
porod_mw_errornull
pddf_i00.2708
pddf_i0_errornull
guinier_i00.28
guinier_i0_error0.00032
pddf_rg3.81
pddf_rg_errornull
guinier_rg3.72
guinier_rg_error0.064
pddf_dmax13.69
pddf_dmax_errornull
porod_volume176.7
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first12
guinier_point_last33
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDD47_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDD47
statussuccess
started_at2026-08-11T15:21:38.447682+00:00
finished_at2026-08-11T15:21:46.050244+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDD47",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants.",
    "publication": {
      "title": "FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants.",
      "author_list": "Grinter R, Hay ID, Song J, Wang J, Teng D, Dhanesakaran V, Wilksch JJ, Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T",
      "journal": "PLoS Biol",
      "doi": "10.1371/journal.pbio.2006026",
      "pmid": "30071011",
      "published_date": "2018 Aug"
    },
    "status": "released",
    "submitted_date": "2018-05-19",
    "released_date": "2018-06-13"
  },
  "pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDD47.out",
  "intensities_data": "https://www.sasbdb.org/media/intensities_files/SASDD47.dat",
  "intensities_log_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDD47_dat_img.png",
  "intensities_kratky_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDD47_kratky_img.png",
  "pddf_plot": "https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDD47_pofr_img.png",
  "intensities_guinier_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDD47_guinier_img.png",
  "sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDD47.sascif",
  "experiment": {
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      "detector": {
        "type": "Dectris",
        "name": "Pilatus 1M",
        "resolution": 172.0
      },
      "name": "Australian  Synchrotron",
      "city": "Melbourne",
      "country": "Australia",
      "beamline_name": "SAXS/WAXS",
      "beam_geometry": "Point",
      "type_of_source": "X-ray synchrotron",
      "point_source": true,
      "line_collimation": null,
      "sample_path_length": null,
      "line_collimation_slitlength": null,
      "line_collimation_integrationwidth": null,
      "xray_energy": null,
      "beam_profile_ah": null,
      "beam_profile_al": null
    },
    "sample": {
      "molecule": [
        {
          "long_name": "Ferredoxin protease E83A mutant",
          "short_name": "FusC E83A",
          "sequence": "EEIKSPLPVFKEGTLANGFRYTLVQLEGPKTRVDIRLIVDVGSIDEKDNESGVAH\r\nMVAHMVFRASDAFPQGVSTELHKQGWGRGQSYNAVTNYERTMYMMSPPKGNLDLGATLQALSQMTGHAKLLQSDLDDERK\r\nIILEEWRGKLGVAERMNQQRVQAIRHDSRYPSRPVIGTEESINDTPASVLQDFYQRWYHPSNMRLMIIGDITPADAEREI\r\nQRYFAALPNVAVPTRDYYEPLLKPQLKVARLQDSQSGSSQVSFVYRFNDKDAFGQSEYRHRLLTQITMSAVTRQVRRQKA\r\nELPQDASSLVVRKSDIGKTTAALGFFANVMPGGHDAAISAVLKEIERFKRYPLNEQDITEITSDIREVAQRMSVTPETRE\r\nFADWVQQLTIVWQQDRPYVGSQQRGKDALEALDTIKGEDVNRHWQRWLASPDTLAQFSVPGATPFTLPKPDAISKLQKQW\r\nALATLAPLRLEEKKIIPELPSVTQSGKRTAVKTFAAQKVEQWQLSNGDRVVWLRAPEAGKKVYLTATSQAGFMATAMNPW\r\nQAQLASQLVNQSGPATWSGESLSNWKKEKTLSLSIDQEADQLTLSGTAPTEQLASLFGLYRELNVAPGIDPDVMKESMMS\r\nLARQKANDDQSVGGKRASEMTKLRFGEPAWQQPEIAELKKISAPALLSQWHKAASAPVTYYLIADMPATQLLPQVERYLA\r\nTIPRQPASEVKQHLALSGKREATSAINVEPRADILTWSFTPHAWTPQAAVQVSIARNIASKYLKTSLRDDALGIYRMRVD\r\nSELEDKKQRIETEVSFTSAPERAQELWTLAEQAFSELPTKITQQDVDEQKAQFIRAEKGRQGDLTTIQRRLILSYRHYND\r\nPRYLSNASKLADSITLESVRAMSAKLYNPDNRVLYITLPQEVKE",
          "organism": "Pectobacterium atrosepticum SCRI1043",
          "uniprot_code": "Q6D8U3",
          "uniprot_range_first": 26,
          "uniprot_range_last": 924,
          "oligomerization": "monomer",
          "molecular_type": "protein",
          "uniprot_sequence": "MNWKKCCWLSLTAVGLLAGSVVSQAEEIKSPLPVFKEGTLANGFRYTLVQLEGPKTRVDI\nRLIVDVGSIDEKDNESGVAHMVEHMVFRASDAFPQGVSTELHKQGWGRGQSYNAVTNYER\nTMYMMSPPKGNLDLGATLQALSQMTGHAKLLQSDLDDERKIILEEWRGKLGVAERMNQQR\nVQAIRHDSRYPSRPVIGTEESINDTPASVLQDFYQRWYHPSNMRLMIIGDITPADAEREI\nQRYFAALPNVAVPTRDYYEPLLKPQLKVARLQDSQSGSSQVSFVYRFNDKDAFGQSEYRH\nRLLTQITMSAVTRQVRRQKAELPQDASSLVVRKSDIGKTTAALGFFANVMPGGHDAAISA\nVLKEIERFKRYPLNEQDITEITSDIREVAQRMSVTPETREFADWVQQLTIVWQQDRPYVG\nSQQRGKDALEALDTIKGEDVNRHWQRWLASPDTLAQFSVPGATPFTLPKPDAISKLQKQW\nALATLAPLRLEEKKIIPELPSVTQSGKRTAVKTFAAQKVEQWQLSNGDRVVWLRAPEAGK\nKVYLTATSQAGFMATAMNPWQAQLASQLVNQSGPATWSGESLSNWKKEKTLSLSIDQEAD\nQLTLSGTAPTEQLASLFGLYRELNVAPGIDPDVMKESMMSLARQKANDDQSVGGKRASEM\nTKLRFGEPAWQQPEIAELKKISAPALLSQWHKAASAPVTYYLIADMPATQLLPQVERYLA\nTIPRQPASEVKQHLALSGKREATSAINVEPRADILTWSFTPHAWTPQAAVQVSIARNIAS\nKYLKTSLRDDALGIYRMRVDSELEDKKQRIETEVSFTSAPERAQELWTLAEQAFSELPTK\nITQQDVDEQKAQFIRAEKGRQGDLTTIQRRLILSYRHYNDPRYLSNASKLADSITLESVR\nAMSAKLYNPDNRVLYITLPQEVKE",
          "mw": 101.195,
          "total_mw": 101.195,
          "number_molecules": 1,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        },
        {
          "long_name": "Arabidopsis ferredoxin 2",
          "short_name": "Ara_Fer2",
          "sequence": "ATYKVKFITPEGELEVECDDDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSVDQSDQSFLDDEQIGEGFVLTCAAYPTSDVTIETHKEEAIMLEHHHHHH",
          "organism": "Arabidopsis thaliana",
          "uniprot_code": "P16972",
          "uniprot_range_first": 53,
          "uniprot_range_last": 145,
          "oligomerization": "monomer",
          "molecular_type": "protein",
          "uniprot_sequence": "MASTALSSAIVGTSFIRRSPAPISLRSLPSANTQSLFGLKSGTARGGRVTAMATYKVKFI\nTPEGELEVECDDDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSVDQSDQSFLDDEQ\nIGEGFVLTCAAYPTSDVTIETHKEEDIV",
          "mw": 11.33,
          "total_mw": 11.33,
          "number_molecules": 1,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        }
      ],
      "buffer": {
        "name": "20 mM Tris, 150 mM NaCl",
        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 7.8,
        "deuteration": null
      },
      "purity_method": null,
      "name": "The ferredoxin protease, FusC, E83A mutant + 100 µM Arabidopsis ferredoxin",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": null,
            "address": "Melbourne, Australia",
            "full_name": "Monash University",
            "webpage": "http://www.monash.edu/"
          }
        ],
        "contributor_name": "Grinter",
        "contributor_surname": "Grinter",
        "orcid": "https://orcid.org/0000-0002-8195-5348"
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2017-10-26",
    "storage_temperature": 20.0,
    "cell_temperature": 20.0,
    "exposure_time": null,
    "number_of_frames": null,
    "wavelength": 0.103,
    "sample_detector_distance": 1.28,
    "concentration_min": null,
    "concentration_max": 3.0,
    "sample_volume": null,
    "flow_rate": null,
    "s_min": 0.114,
    "s_max": 3.038,
    "total_exposure_time": null,
    "seccolumn": null
  },
  "fits": [],
  "estimated_volume_method": null,
  "pddf_software": "ATSAS GNOM",
  "pddf_software_version": "5.0",
  "i0_calibration_standard": null,
  "description": "The FusC E83A mutant (30 µM) in the presence of 100 µM Arabidopsis ferredoxin. The background subtraction included 100 µM Arabidopsis ferredoxin in buffer.",
  "experiment_description": "Synchrotron SAXS data from solutions of ferredoxin protease, FusC, E83A mutant + 100 µM Arabidopsis ferredoxin in 20 mM Tris, 150 mM NaCl, pH 7.8 were collected on the SAXS/WAXS beam line at the Australian Synchrotron storage ring (Melbourne, Australia) using a Pilatus 1M detector at a sample-detector distance of 1.3 m and at a wavelength of λ = 0.103 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.00 mg/ml was measured at 20°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.",
  "tags": [],
  "intensity_unit": "arbitrary",
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  "experimental_mw_error": null,
  "guinier_i0_mw": null,
  "guinier_i0_mw_error": null,
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  "pddf_dmax": 13.69,
  "pddf_dmax_error": null,
  "porod_volume": 176.7,
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  "estimated_volume": null,
  "estimated_volume_error": null,
  "guinier_point_first": 12,
  "guinier_point_last": 33,
  "pddf_point_first": null,
  "pddf_point_last": null,
  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDD47_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2019-12-06T13:07:15.624532+01:00",
  "bragg_peak": []
}
View the complete manifest.json source
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