SASDVB8

C-terminal truncation mutant of N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2025-01-02T12:10:48.459172+01:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · C-terminal truncation mutant of N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF

Concentration5.0 – 5.0 Buffer / pH50 mM Tris, 200 mM NaCl / 8.0
Experimental temperature20.0 Facility / beamlineInstitute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure / Anton Paar SAXSpoint 2.0
Wavelength0.134 nmExposure15.0 s × 60

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF (Δ444-462)
View sequence
MGSSHHHHHHSSGENLYFQGHMATQSSTELPQINMTTAEPTSANKRTYPWVKLPHPYLTSYAIHVVSESTPRVLQLRLHDDQKGQALPEPLHSASLTYTDIAFDEAAQEIPDNDNSPWARSRRAPGTSFHWTGQEPPTLGQIWNVIHALFLTYPQHEIVRLDLNGSGKDIIREECLRTGLAVPFPSPRVPFGTENRPSETDTLILLRSAFWQGAGSPVGPRPIWAVDHGIHGLLRRSGSSYPPLAQNYEFSMKFPSERIYTRHPIRPQKPAPGSLVYSRYIPHLDQHFSLMVVDWQNEEHLQLFHKWQNDPRVAKGWNETGDLEHHRNYLRQLHEDKHVLCLFGRFDDFPFSYFEVYWAKEDHYGAHYDAGDYDRGRHSLVGESSVRGAYRVNAWWSSLIHYIFLDEPRTMCVVGEPKATNTTVLSYENAHGLTVQKYVDLGHKRSVHVYCSREKWFQLCPLFW
proteinAspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)Q4WF551–443dimerMolecule count 253.495 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1501[3]0.01235556–0.3027259 1/AHas uncertainty columnMissing 041sasbdb/entries/b8/sasdvb8/source/SASDVB8.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)15.0—Å
i0Guinier0.276504—arbitrary
i0P(r)0.2812—arbitrary
mwExperimental109.1—kDa
mwPorod118.0—kDa
porod_volumePorod189.0—ų
rgGuinier3.4520.208Å
rgP(r)3.68—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

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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, 200 mM NaClBuffer concentration—
pH8.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2023-01-18Storage / measurement temperature20.0 / 20.0
Exposure time15.0Frames60
Wavelength0.134Sample-to-detector distance0.571
SourceX-ray in houseDetectorEiger R 1M
Facility / beamlineInstitute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure / Anton Paar SAXSpoint 2.0 · Vestec, Czech Republic
q range0.124 – 3.027Sample volume / flow rate400.0 / 0.05

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:156 field values
Field pathRaw value
codeSASDVB8
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleSidF, a dual substrate N5-acetyl-N5-hydroxy-L-ornithine transacetylase involved in Aspergillus fumigatus siderophore biosynthesis
project.publication.titleSidF, a dual substrate N5-acetyl-N5-hydroxy-L-ornithine transacetylase involved in Aspergillus fumigatus siderophore biosynthesis
project.publication.author_listPoonsiri T, Stransky J, Demitri N, Haas H, Cianci M, Benini S
project.publication.journalJournal of Structural Biology: X
project.publication.doi10.1016/j.yjsbx.2024.100119
project.publication.pmidnull
project.publication.published_date2025 Jun
project.statusreleased
project.submitted_date2024-10-21
project.released_date2025-01-02
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDVB8.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDVB8.dat
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intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDVB8_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDVB8_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDVB8_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDVB8.sascif
experiment.instrument.detector.typenull
experiment.instrument.detector.nameEiger R 1M
experiment.instrument.detector.resolution0.75
experiment.instrument.nameInstitute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure
experiment.instrument.cityVestec
experiment.instrument.countryCzech Republic
experiment.instrument.beamline_nameAnton Paar SAXSpoint 2.0
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_nameN(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF (Δ444-462)
experiment.sample.molecule[0].short_nameSidF C-trim
experiment.sample.molecule[0].sequenceMGSSHHHHHHSSGENLYFQGHMATQSSTELPQINMTTAEPTSANKRTYPWVKLPHPYLTSYAIHVVSESTPRVLQLRLHDDQKGQALPEPLHSASLTYTDIAFDEAAQEIPDNDNSPWARSRRAPGTSFHWTGQEPPTLGQIWNVIHALFLTYPQHEIVRLDLNGSGKDIIREECLRTGLAVPFPSPRVPFGTENRPSETDTLILLRSAFWQGAGSPVGPRPIWAVDHGIHGLLRRSGSSYPPLAQNYEFSMKFPSERIYTRHPIRPQKPAPGSLVYSRYIPHLDQHFSLMVVDWQNEEHLQLFHKWQNDPRVAKGWNETGDLEHHRNYLRQLHEDKHVLCLFGRFDDFPFSYFEVYWAKEDHYGAHYDAGDYDRGRHSLVGESSVRGAYRVNAWWSSLIHYIFLDEPRTMCVVGEPKATNTTVLSYENAHGLTVQKYVDLGHKRSVHVYCSREKWFQLCPLFW
experiment.sample.molecule[0].organismAspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)
experiment.sample.molecule[0].uniprot_codeQ4WF55
experiment.sample.molecule[0].uniprot_range_first1
experiment.sample.molecule[0].uniprot_range_last443
experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMATQSSTELPQINMTTAEPTSANKRTYPWVKLPHPYLTSYAIHVVSESTPRVLQLRLHDD QKGQALPEPLHSASLTYTDIAFDEAAQEIPDNDNSPWARSRRAPGTSFHWTGQEPPTLGQ IWNVIHALFLTYPQHEIVRLDLNGSGKDIIREECLRTGLAVPFPSPRVPFGTENRPSETD TLILLRSAFWQGAGSPVGPRPIWAVDHGIHGLLRRSGSSYPPLAQNYEFSMKFPSERIYT RHPIRPQKPAPGSLVYSRYIPHLDQHFSLMVVDWQNEEHLQLFHKWQNDPRVAKGWNETG DLEHHRNYLRQLHEDKHVLCLFGRFDDFPFSYFEVYWAKEDHYGAHYDAGDYDRGRHSLV GESSVRGAYRVNAWWSSLIHYIFLDEPRTMCVVGEPKATNTTVLSYENAHGLTVQKYVDL GHKRSVHVYCSREKWFQLCPLFWDGRERPLESSDRMAWDAKL
experiment.sample.molecule[0].mw53.495
experiment.sample.molecule[0].total_mw106.99
experiment.sample.molecule[0].number_molecules2
experiment.sample.molecule[0].complex_stateFalse
experiment.sample.molecule[0].deuterationnull
experiment.sample.molecule[0].molecule_sourcebiological
experiment.sample.molecule[0].molecule_descriptionThe protein construct used for SAXS contains a non-native polyhistidine tag, with additional non-native amino acids at the N-terminus (MGSSHHHHHHSSGENLYFQGH).
experiment.sample.buffer.name50 mM Tris, 200 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.ph8.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameC-terminal truncation mutant of N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF
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_nameMahidol University
experiment.contributor[0].affiliation[0].webpagehttps://mahidol.ac.th/
experiment.contributor[0].contributor_nameThanalai
experiment.contributor[0].contributor_surnamePoonsiri
experiment.contributor[0].orcid
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2023-01-18
experiment.storage_temperature20.0
experiment.cell_temperature20.0
experiment.exposure_time15.0
experiment.number_of_frames60
experiment.wavelength0.134
experiment.sample_detector_distance0.571
experiment.concentration_min5.0
experiment.concentration_max5.0
experiment.sample_volume400.0
experiment.flow_rate0.05
experiment.s_min0.124
experiment.s_max3.027
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].softwareCORAL
fits[0].models[0].pdb_link[]
fits[0].models[0].model_titlenull
fits[0].models[0].type_of_modelmix
fits[0].models[0].software_version5
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fits[0].models[0].model_mw101.3
fits[0].models[0].bead_radius1.9
fits[0].models[0].lognull
fits[0].models[0].symmetrynull
fits[0].models[0].commentnull
fits[0].models[0].user1131
fits[0].fit_unit1/A
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fits[0].softwareCORAL
fits[0].chi_square_value1.87
fits[0].p_value0.0
fits[0].fit_residual_plotSASDVB8_fit1_fitresiduals_img.png
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fits[0].software_version5
fits[0].description
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionSAXS data from solutions of C-terminal truncated sidF in 50 mM Tris, 200 mM NaCl, pH 8 were collected using an Anton Paar SAXSpoint 2.0 instrument at the Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure (Vestec, Czech Republic) equipped with an Eiger R 1M detector at a sample-detector distance of 0.6 m and at a wavelength of λ = 0.134 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). A sample concentration at 5 mg/ml was measured at 20°C. 60 successive 15 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_mw109.1
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw118.0
porod_mw_errornull
pddf_i00.2812
pddf_i0_errornull
guinier_i00.276504
guinier_i0_errornull
pddf_rg3.68
pddf_rg_errornull
guinier_rg3.452
guinier_rg_error0.208
pddf_dmax15.0
pddf_dmax_errornull
porod_volume189.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first5
guinier_point_last43
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDVB8_datloglog_img.png
symmetrynull
last_modified2025-01-02T12:10:48.459172+01:00
bragg_peak[]
manifest.json:34 field values
Field pathRaw value
codeSASDVB8
statussuccess
started_at2026-08-11T16:33:13.507421+00:00
finished_at2026-08-11T16:33:22.384744+00:00
source_last_modified2025-01-02T12:10:48.459172+01:00
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View the complete summary.json source
{
  "code": "SASDVB8",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "SidF, a dual substrate N5-acetyl-N5-hydroxy-L-ornithine transacetylase involved in Aspergillus fumigatus siderophore biosynthesis",
    "publication": {
      "title": "SidF, a dual substrate N5-acetyl-N5-hydroxy-L-ornithine transacetylase involved in Aspergillus fumigatus siderophore biosynthesis",
      "author_list": "Poonsiri T, Stransky J, Demitri N, Haas H, Cianci M, Benini S",
      "journal": "Journal of Structural Biology: X",
      "doi": "10.1016/j.yjsbx.2024.100119",
      "pmid": null,
      "published_date": "2025 Jun"
    },
    "status": "released",
    "submitted_date": "2024-10-21",
    "released_date": "2025-01-02"
  },
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  "pddf_plot": "https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDVB8_pofr_img.png",
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  "experiment": {
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        "type": null,
        "name": "Eiger R 1M",
        "resolution": 0.75
      },
      "name": "Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure",
      "city": "Vestec",
      "country": "Czech Republic",
      "beamline_name": "Anton Paar SAXSpoint 2.0",
      "beam_geometry": null,
      "type_of_source": "X-ray in house",
      "point_source": null,
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    },
    "sample": {
      "molecule": [
        {
          "long_name": "N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF (Δ444-462)",
          "short_name": "SidF C-trim",
          "sequence": "MGSSHHHHHHSSGENLYFQGHMATQSSTELPQINMTTAEPTSANKRTYPWVKLPHPYLTSYAIHVVSESTPRVLQLRLHDDQKGQALPEPLHSASLTYTDIAFDEAAQEIPDNDNSPWARSRRAPGTSFHWTGQEPPTLGQIWNVIHALFLTYPQHEIVRLDLNGSGKDIIREECLRTGLAVPFPSPRVPFGTENRPSETDTLILLRSAFWQGAGSPVGPRPIWAVDHGIHGLLRRSGSSYPPLAQNYEFSMKFPSERIYTRHPIRPQKPAPGSLVYSRYIPHLDQHFSLMVVDWQNEEHLQLFHKWQNDPRVAKGWNETGDLEHHRNYLRQLHEDKHVLCLFGRFDDFPFSYFEVYWAKEDHYGAHYDAGDYDRGRHSLVGESSVRGAYRVNAWWSSLIHYIFLDEPRTMCVVGEPKATNTTVLSYENAHGLTVQKYVDLGHKRSVHVYCSREKWFQLCPLFW",
          "organism": "Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)",
          "uniprot_code": "Q4WF55",
          "uniprot_range_first": 1,
          "uniprot_range_last": 443,
          "oligomerization": "dimer",
          "molecular_type": "protein",
          "uniprot_sequence": "MATQSSTELPQINMTTAEPTSANKRTYPWVKLPHPYLTSYAIHVVSESTPRVLQLRLHDD\nQKGQALPEPLHSASLTYTDIAFDEAAQEIPDNDNSPWARSRRAPGTSFHWTGQEPPTLGQ\nIWNVIHALFLTYPQHEIVRLDLNGSGKDIIREECLRTGLAVPFPSPRVPFGTENRPSETD\nTLILLRSAFWQGAGSPVGPRPIWAVDHGIHGLLRRSGSSYPPLAQNYEFSMKFPSERIYT\nRHPIRPQKPAPGSLVYSRYIPHLDQHFSLMVVDWQNEEHLQLFHKWQNDPRVAKGWNETG\nDLEHHRNYLRQLHEDKHVLCLFGRFDDFPFSYFEVYWAKEDHYGAHYDAGDYDRGRHSLV\nGESSVRGAYRVNAWWSSLIHYIFLDEPRTMCVVGEPKATNTTVLSYENAHGLTVQKYVDL\nGHKRSVHVYCSREKWFQLCPLFWDGRERPLESSDRMAWDAKL",
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          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": "The protein construct used for SAXS contains a non-native polyhistidine tag, with additional non-native amino acids at the N-terminus (MGSSHHHHHHSSGENLYFQGH)."
        }
      ],
      "buffer": {
        "name": "50 mM Tris, 200 mM NaCl",
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        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 8.0,
        "deuteration": null
      },
      "purity_method": null,
      "name": "C-terminal truncation mutant of N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": null,
            "address": "Thailand",
            "full_name": "Mahidol University",
            "webpage": "https://mahidol.ac.th/"
          }
        ],
        "contributor_name": "Thanalai",
        "contributor_surname": "Poonsiri",
        "orcid": ""
      }
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    "concentration_method": null,
    "concentration_unit": null,
    "date": "2023-01-18",
    "storage_temperature": 20.0,
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          "comment": null,
          "user": 1131
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      "fit_unit": "1/A",
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      "software_version": "5",
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  "guinier_point_last": 43,
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  "last_modified": "2025-01-02T12:10:48.459172+01:00",
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}
View the complete manifest.json source
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