SASDVY7

Glutamine C‐methyltransferase without cobalamin from Methanoculleus thermophilus

Data type: SASBDB experimental data Status: Published Curve type: SEC-SAS Last updated: 2026-05-27T09:45:48.001805+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Glutamine C‐methyltransferase without cobalamin from Methanoculleus thermophilus

Concentration— – 5.0 Buffer / pH50 mM Tris, 300 mM NaCl, 5% glycerol / 8.0
Experimental temperature20.0 Facility / beamlineSOLEIL / SWING
Wavelength0.1033 nmExposure0.99 s × 646

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
B12-binding domain/radical SAM domain protein, MJ_0865 family
View sequence
MDITIFSPGIYTYGAMLIGGVLRDAGHEVTLTRTPEVPEGSLLLASLFSTQHLLDPKIRSLVRRHRERGGTVYVGGPVSAVPEIVLRELAPDAVVVGEGEETVVRLAEEGASETLPGIAYLDGDQAVVTAPAPPAPIDRPLPLIPEDIGSQSIRGASAYIETHRGCIGGCTFCQVPRFFGREVRSRPLESIIEEVKAFRAAGAKRLSISGGTGSLYGSHGCEMNPGAFIALLRGMAEVMGPKNVSAPDIRVDCITDEILDAIRQYTIGWVFFGIESGSNRVLRQMGKGATVREVEEAVERCREHGLHVAGSFIVGYPGETERDYEATKDLVAALSLDDVFISSAEPIPGTPLADLVIRTPRDKNPAFMPHTGEYRALHLTESEARCFDLMMHADMYRPQIRLVTDEVYAAYLAEAKKQGEDIRAATELILRYAQR
proteinMethanoculleus thermophilusWP_06695761–435monomerMolecule count 149.962 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11092[3]0.003648777–0.4999793 1/AHas uncertainty columnMissing 021sasbdb/entries/y7/sasdvy7/source/SASDVY7.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)10.4—Å
i0Guinier0.0220185—arbitrary
i0P(r)0.0221—arbitrary
mwExperimental50.3—kDa
mwPorod53.0—kDa
porod_volumePorod85.0—ų
rgGuinier2.6250.086Å
rgP(r)2.67—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, 300 mM NaCl, 5% glycerolBuffer concentration—
pH8.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2024-09-18Storage / measurement temperature6.0 / 20.0
Exposure time0.99Frames646
Wavelength0.1033Sample-to-detector distance2.0
SourceX-ray synchrotronDetectorEiger 4M
Facility / beamlineSOLEIL / SWING · Saint-Aubin, France
q range0.036 – 5.0Sample volume / flow rate50.0 / 0.25

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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summarysasbdb/entries/y7/sasdvy7/source/summary.jsondownloaded82872eaa40128187b7c8df1b68dcac8bd17ad799a2e42d8e606121e2dc2fafeeae54DownloadView source fileSource site
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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
codeSASDVY7
statusPublished
type_of_curveSEC-SAS
angular_unit1/A
project.titleInsights into the stereochemical mechanism of the B(12)-dependent radical SAM glutamine C- methyltransferase (QCMT).
project.publication.titleInsights into the stereochemical mechanism of the B(12)-dependent radical SAM glutamine C- methyltransferase (QCMT).
project.publication.author_listBourdin T, Guillot A, Mauger M, Lefranc B, Gervason S, Glousieau M, Grimaldi S, Leprince J, Thureau A, Benjdia A, Berteau O
project.publication.journalCommun Biol
project.publication.doi10.1038/s42003-026-10234-8
project.publication.pmid42168528
project.publication.published_date2026 May 21
project.statusreleased
project.submitted_date2024-05-17
project.released_date2026-05-17
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intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDVY7_fit1.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDVY7_fit1_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDVY7_fit1_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDVY7_pofr_img.png
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experiment.instrument.detector.typenull
experiment.instrument.detector.nameEiger 4M
experiment.instrument.detector.resolution75.0
experiment.instrument.nameSOLEIL
experiment.instrument.citySaint-Aubin
experiment.instrument.countryFrance
experiment.instrument.beamline_nameSWING
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
experiment.instrument.line_collimation_integrationwidthnull
experiment.instrument.xray_energynull
experiment.instrument.beam_profile_ahnull
experiment.instrument.beam_profile_alnull
experiment.sample.molecule[0].long_nameB12-binding domain/radical SAM domain protein, MJ_0865 family
experiment.sample.molecule[0].short_nameQCMTMe
experiment.sample.molecule[0].sequenceMDITIFSPGIYTYGAMLIGGVLRDAGHEVTLTRTPEVPEGSLLLASLFST QHLLDPKIRSLVRRHRERGGTVYVGGPVSAVPEIVLRELAPDAVVVGEGE ETVVRLAEEGASETLPGIAYLDGDQAVVTAPAPPAPIDRPLPLIPEDIGS QSIRGASAYIETHRGCIGGCTFCQVPRFFGREVRSRPLESIIEEVKAFRA AGAKRLSISGGTGSLYGSHGCEMNPGAFIALLRGMAEVMGPKNVSAPDIR VDCITDEILDAIRQYTIGWVFFGIESGSNRVLRQMGKGATVREVEEAVER CREHGLHVAGSFIVGYPGETERDYEATKDLVAALSLDDVFISSAEPIPGT PLADLVIRTPRDKNPAFMPHTGEYRALHLTESEARCFDLMMHADMYRPQI RLVTDEVYAAYLAEAKKQGEDIRAATELILRYAQR
experiment.sample.molecule[0].organismMethanoculleus thermophilus
experiment.sample.molecule[0].uniprot_codeWP_0669576
experiment.sample.molecule[0].uniprot_range_first1
experiment.sample.molecule[0].uniprot_range_last435
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMDITIFSPGIYTYGAMLIGGVLRDAGHEVTLTRTPEVPEGSLLLASLFSTQHLLDPKIRS LVRRHRERGGTVYVGGPVSAVPEIVLRELAPDAVVVGEGEETVVRLAEEGASETLPGIAY LDGDQAVVTAPAPPAPIDRPLPLIPEDIGSQSIRGASAYIETHRGCIGGCTFCQVPRFFG REVRSRPLESIIEEVKAFRAAGAKRLSISGGTGSLYGSHGCEMNPGAFIALLRGMAEVMG PKNVSAPDIRVDCITDEILDAIRQYTIGWVFFGIESGSNRVLRQMGKGATVREVEEAVER CREHGLHVAGSFIVGYPGETERDYEATKDLVAALSLDDVFISSAEPIPGTPLADLVIRTP RDKNPAFMPHTGEYRALHLTESEARCFDLMMHADMYRPQIRLVTDEVYAAYLAEAKKQGE DIRAATELILRYAQR
experiment.sample.molecule[0].mw49.962
experiment.sample.molecule[0].total_mw49.962
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_descriptionApo protein with an Fe-S cluster. The protein construct used for SAXS contains an additional amino acid extension at the N-terminus (MASWSHPQFEKSGGGGGENLYFQGH).
experiment.sample.buffer.name50 mM Tris, 300 mM NaCl, 5% glycerol
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.nameGlutamine C‐methyltransferase without cobalamin from Methanoculleus thermophilus
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_nameSoleil
experiment.contributor[0].affiliation[0].addressSaint-Aubin, France
experiment.contributor[0].affiliation[0].full_nameSoleil Synchrotron
experiment.contributor[0].affiliation[0].webpagehttp://www.synchrotron-soleil.fr/
experiment.contributor[0].contributor_nameAurélien
experiment.contributor[0].contributor_surnameThureau
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2024-09-18
experiment.storage_temperature6.0
experiment.cell_temperature20.0
experiment.exposure_time0.99
experiment.number_of_frames646
experiment.wavelength0.1033
experiment.sample_detector_distance2.0
experiment.concentration_minnull
experiment.concentration_max5.0
experiment.sample_volume50.0
experiment.flow_rate0.25
experiment.s_min0.036
experiment.s_max5.0
experiment.total_exposure_timenull
experiment.seccolumn46
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fits[0].models[0].softwareAlphaFold
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fits[0].softwareCRYSOL
fits[0].chi_square_value1.371
fits[0].p_value0.0
fits[0].fit_residual_plotSASDVY7_fit1_fitresiduals_img.png
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fits[0].fit_lognull
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fits[0].description
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionnull
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from solutions of glutamine C‐methyltransferase without cobalamin in 50 mM Tris, 300 mM NaCl, 5% glycerol, pH 8 were collected on the SWING beam line at SOLEIL (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 5 mg/ml was injected at a 0.25 ml/min flow rate onto a Cytiva Superdex 200 5/150 column at 20°C. 646 successive 0.990 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_mw50.3
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw53.0
porod_mw_errornull
pddf_i00.0221
pddf_i0_errornull
guinier_i00.0220185
guinier_i0_errornull
pddf_rg2.67
pddf_rg_errornull
guinier_rg2.625
guinier_rg_error0.086
pddf_dmax10.4
pddf_dmax_errornull
porod_volume85.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first11
guinier_point_last83
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDVY7_fit1_datloglog_img.png
symmetrynull
last_modified2026-05-27T09:45:48.001805+02:00
bragg_peak[]
manifest.json:34 field values
Field pathRaw value
codeSASDVY7
statussuccess
started_at2026-08-11T15:42:56.216377+00:00
finished_at2026-08-11T15:43:04.502801+00:00
source_last_modified2026-05-27T09:45:48.001805+02:00
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View the complete summary.json source
{
  "code": "SASDVY7",
  "status": "Published",
  "type_of_curve": "SEC-SAS",
  "angular_unit": "1/A",
  "project": {
    "title": "Insights into the stereochemical mechanism of the B(12)-dependent radical SAM glutamine C- methyltransferase (QCMT).",
    "publication": {
      "title": "Insights into the stereochemical mechanism of the B(12)-dependent radical SAM glutamine C- methyltransferase (QCMT).",
      "author_list": "Bourdin T, Guillot A, Mauger M, Lefranc B, Gervason S, Glousieau M, Grimaldi S, Leprince J, Thureau A, Benjdia A, Berteau O",
      "journal": "Commun Biol",
      "doi": "10.1038/s42003-026-10234-8",
      "pmid": "42168528",
      "published_date": "2026 May 21"
    },
    "status": "released",
    "submitted_date": "2024-05-17",
    "released_date": "2026-05-17"
  },
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  "experiment": {
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      "country": "France",
      "beamline_name": "SWING",
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    "sample": {
      "molecule": [
        {
          "long_name": "B12-binding domain/radical SAM domain protein, MJ_0865 family",
          "short_name": "QCMTMe",
          "sequence": "MDITIFSPGIYTYGAMLIGGVLRDAGHEVTLTRTPEVPEGSLLLASLFST\r\nQHLLDPKIRSLVRRHRERGGTVYVGGPVSAVPEIVLRELAPDAVVVGEGE\r\nETVVRLAEEGASETLPGIAYLDGDQAVVTAPAPPAPIDRPLPLIPEDIGS\r\nQSIRGASAYIETHRGCIGGCTFCQVPRFFGREVRSRPLESIIEEVKAFRA\r\nAGAKRLSISGGTGSLYGSHGCEMNPGAFIALLRGMAEVMGPKNVSAPDIR\r\nVDCITDEILDAIRQYTIGWVFFGIESGSNRVLRQMGKGATVREVEEAVER\r\nCREHGLHVAGSFIVGYPGETERDYEATKDLVAALSLDDVFISSAEPIPGT\r\nPLADLVIRTPRDKNPAFMPHTGEYRALHLTESEARCFDLMMHADMYRPQI\r\nRLVTDEVYAAYLAEAKKQGEDIRAATELILRYAQR",
          "organism": "Methanoculleus thermophilus",
          "uniprot_code": "WP_0669576",
          "uniprot_range_first": 1,
          "uniprot_range_last": 435,
          "oligomerization": "monomer",
          "molecular_type": "protein",
          "uniprot_sequence": "MDITIFSPGIYTYGAMLIGGVLRDAGHEVTLTRTPEVPEGSLLLASLFSTQHLLDPKIRS\r\nLVRRHRERGGTVYVGGPVSAVPEIVLRELAPDAVVVGEGEETVVRLAEEGASETLPGIAY\r\nLDGDQAVVTAPAPPAPIDRPLPLIPEDIGSQSIRGASAYIETHRGCIGGCTFCQVPRFFG\r\nREVRSRPLESIIEEVKAFRAAGAKRLSISGGTGSLYGSHGCEMNPGAFIALLRGMAEVMG\r\nPKNVSAPDIRVDCITDEILDAIRQYTIGWVFFGIESGSNRVLRQMGKGATVREVEEAVER\r\nCREHGLHVAGSFIVGYPGETERDYEATKDLVAALSLDDVFISSAEPIPGTPLADLVIRTP\r\nRDKNPAFMPHTGEYRALHLTESEARCFDLMMHADMYRPQIRLVTDEVYAAYLAEAKKQGE\r\nDIRAATELILRYAQR",
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        "deuteration": null
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      "contrast": null,
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      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": "Soleil",
            "address": "Saint-Aubin, France",
            "full_name": "Soleil Synchrotron",
            "webpage": "http://www.synchrotron-soleil.fr/"
          }
        ],
        "contributor_name": "Aurélien",
        "contributor_surname": "Thureau",
        "orcid": null
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    "concentration_unit": null,
    "date": "2024-09-18",
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  "last_modified": "2026-05-27T09:45:48.001805+02:00",
  "bragg_peak": []
}
View the complete manifest.json source
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