SASDVC4

Shwachman-Bodian-Diamond syndrome protein (SBDS) - wild type

Data type: SASBDB experimental data Status: Published Curve type: SEC-SAS Last updated: 2025-08-04T15:55:11.180598+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Shwachman-Bodian-Diamond syndrome protein (SBDS) - wild type

Concentration— – 11.0 Buffer / pH50 mM Tris pH 8.0, 10% glycerol, 300 mM NaCl, 5 mM MgCl2. / —
Experimental temperature20.0 Facility / beamlinePETRA III / EMBL P12
Wavelength0.124 nmExposure0.5 s × 1800

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Ribosome maturation protein SBDS
View sequence
MSIFTPTNQIRLTNVAVVRMKRAGKRFEIACYKNKVVGWRSGVEKDLDEVLQTHSVFVNVSKGQVAKKEDLISAFGTDDQTEICKQILTKGEVQVSDKERHTQLEQMFRDIATIVADKCVNPETKRPYTVILIERAMKDIHYSVKTNKSTKQQALEVIKQLKEKMKIERAHMRLRFILPVNEGKKLKEKLKPLIKVIESEDYGQQLEIVCLIDPGCFREIDELIKKETKGKGSLEVLNLKDVEEGDEKFE
proteinHomo sapiensQ9Y3A51–250monomerMolecule count 128.763 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11985[3]0.00551512–0.440688 1/AHas uncertainty columnMissing 017sasbdb/entries/c4/sasdvc4/source/SASDVC4.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)11.35—Å
i0Guinier1219.63—arbitrary
i0P(r)9367.068—arbitrary
mwExperimental29.0—kDa
mwPorod29.4—kDa
porod_volumePorod50.0—ų
rgGuinier3.020.118Å
rgP(r)3.04—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 pH 8.0, 10% glycerol, 300 mM NaCl, 5 mM MgCl2.Buffer concentration—
pH—Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2022-04-06Storage / measurement temperature4.0 / 20.0
Exposure time0.5Frames1800
Wavelength0.124Sample-to-detector distance3.0
SourceX-ray synchrotronDetectorPilatus 6M
Facility / beamlinePETRA III / EMBL P12 · DESY; Hamburg, Germany
q range0.055 – 4.407Sample volume / flow rate50.0 / 0.3

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:182 field values
Field pathRaw value
codeSASDVC4
statusPublished
type_of_curveSEC-SAS
angular_unit1/A
project.titleStructural Implications of Missense Point Mutations in Shwachman–Bodian–Diamond Syndrome Protein (SBDS): A Combined SAXS/MD Investigation
project.publication.titleStructural Implications of Missense Point Mutations in Shwachman–Bodian–Diamond Syndrome Protein (SBDS): A Combined SAXS/MD Investigation
project.publication.author_listMattiotti G, Nanna V, Giulini M, Alberga D, Mangiatordi G, Sánchez-Puig N, Saviano M, Tubiana L, Potestio R, Lattanzi G, Siliqi D
project.publication.journalACS Omega
project.publication.doi10.1021/acsomega.5c04764
project.publication.pmidnull
project.publication.published_date2025 Aug 01
project.statusreleased
project.submitted_date2024-07-11
project.released_date2025-08-04
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experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus 6M
experiment.instrument.detector.resolutionnull
experiment.instrument.namePETRA III
experiment.instrument.cityDESY; Hamburg
experiment.instrument.countryGermany
experiment.instrument.beamline_nameEMBL P12
experiment.instrument.beam_geometrynull
experiment.instrument.type_of_sourceX-ray synchrotron
experiment.instrument.point_sourcenull
experiment.instrument.line_collimationnull
experiment.instrument.sample_path_lengthnull
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experiment.instrument.line_collimation_integrationwidthnull
experiment.instrument.xray_energynull
experiment.instrument.beam_profile_ahnull
experiment.instrument.beam_profile_alnull
experiment.sample.molecule[0].long_nameRibosome maturation protein SBDS
experiment.sample.molecule[0].short_nameSBDS
experiment.sample.molecule[0].sequenceMSIFTPTNQIRLTNVAVVRMKRAGKRFEIACYKNKVVGWRSGVEKDLDEVLQTHSVFVNVSKGQVAKKEDLISAFGTDDQTEICKQILTKGEVQVSDKERHTQLEQMFRDIATIVADKCVNPETKRPYTVILIERAMKDIHYSVKTNKSTKQQALEVIKQLKEKMKIERAHMRLRFILPVNEGKKLKEKLKPLIKVIESEDYGQQLEIVCLIDPGCFREIDELIKKETKGKGSLEVLNLKDVEEGDEKFE
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeQ9Y3A5
experiment.sample.molecule[0].uniprot_range_first1
experiment.sample.molecule[0].uniprot_range_last250
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMSIFTPTNQIRLTNVAVVRMKRAGKRFEIACYKNKVVGWRSGVEKDLDEVLQTHSVFVNV SKGQVAKKEDLISAFGTDDQTEICKQILTKGEVQVSDKERHTQLEQMFRDIATIVADKCV NPETKRPYTVILIERAMKDIHYSVKTNKSTKQQALEVIKQLKEKMKIERAHMRLRFILPV NEGKKLKEKLKPLIKVIESEDYGQQLEIVCLIDPGCFREIDELIKKETKGKGSLEVLNLK DVEEGDEKFE
experiment.sample.molecule[0].mw28.763
experiment.sample.molecule[0].total_mw28.763
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_description
experiment.sample.buffer.name50 mM Tris pH 8.0, 10% glycerol, 300 mM NaCl, 5 mM MgCl2.
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.phnull
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experiment.sample.purity_methodnull
experiment.sample.nameShwachman-Bodian-Diamond syndrome protein (SBDS) - wild type
experiment.sample.ext_coefficientnull
experiment.sample.contrastnull
experiment.sample.specific_volnull
experiment.sample.dry_volnull
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experiment.contributor[0].affiliation[0].short_namenull
experiment.contributor[0].affiliation[0].addressBari, Italy
experiment.contributor[0].affiliation[0].full_nameCNR - Institute of Crystallography, Bari, Italy
experiment.contributor[0].affiliation[0].webpagehttp://www.ba.ic.cnr.it
experiment.contributor[0].contributor_nameDritan
experiment.contributor[0].contributor_surnameSiliqi
experiment.contributor[0].orcidhttps://orcid.org/0000-0003-1415-8725
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experiment.concentration_unitnull
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experiment.storage_temperature4.0
experiment.cell_temperature20.0
experiment.exposure_time0.5
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experiment.wavelength0.124
experiment.sample_detector_distance3.0
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experiment.s_min0.055
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experiment.total_exposure_timenull
experiment.seccolumn3
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fits[0].p_value0.0
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pddf_softwareScÅtter
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i0_calibration_standardnull
descriptionnull
experiment_descriptionStructural characterization of human SBDS was performed using size-exclusion chromatography coupled to small-angle X-ray scattering (SEC-SAXS), collected at the EMBL P12 beamline, at PETRA III (Hamburg, Germany), using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm. SEC-SAXS was performed at 20° using a Superdex 75 Increase 5/150 GL size-exclusion column at a flow of 0.3 mL/min and 50 mM Tris-HCl pH 8.0, 10% glycerol, 300 mM NaCl, and 5 mM MgCl2 as running buffer. 50 µL for the sample at concentrations of 11.0 mg/mL was injected and 1800 frames (with 0.5 s exposure time per frame) were collected. Each unsubtracted data frame was normalized to the intensity of the transmitted beam and radially averaged using integrated software available at the beamline. Chromixs software was used to select the frames corresponding to the scattering of the sample and the frames corresponding to the appropriate solvent blank. The resulting subtracted frames were scaled and averaged to generate the final SAXS profile. The flexibility study for SBDS-wt mutant construct was performed using the online version of the program MultiFoXS, described by a 3-state model (closed, stretched and relaxt) to be compared for the three known missense mutants.
tags[]
intensity_unitarbitrary
experimental_mw29.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw29.4
porod_mw_errornull
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pddf_rg_errornull
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pddf_dmax11.35
pddf_dmax_errornull
porod_volume50.0
porod_volume_errornull
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estimated_volume_errornull
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guinier_point_last156
pddf_point_firstnull
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i0_calibration_standard_datanull
intensities_log_log_plotSASDVC4_datloglog_img.png
symmetrynull
last_modified2025-08-04T15:55:11.180598+02:00
bragg_peak[]
manifest.json:34 field values
Field pathRaw value
codeSASDVC4
statussuccess
started_at2026-08-11T14:20:04.895332+00:00
finished_at2026-08-11T14:20:14.863061+00:00
source_last_modified2025-08-04T15:55:11.180598+02:00
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View the complete summary.json source
{
  "code": "SASDVC4",
  "status": "Published",
  "type_of_curve": "SEC-SAS",
  "angular_unit": "1/A",
  "project": {
    "title": "Structural Implications of Missense Point Mutations in Shwachman–Bodian–Diamond Syndrome Protein (SBDS): A Combined SAXS/MD Investigation",
    "publication": {
      "title": "Structural Implications of Missense Point Mutations in Shwachman–Bodian–Diamond Syndrome Protein (SBDS): A Combined SAXS/MD Investigation",
      "author_list": "Mattiotti G, Nanna V, Giulini M, Alberga D, Mangiatordi G, Sánchez-Puig N, Saviano M, Tubiana L, Potestio R, Lattanzi G, Siliqi D",
      "journal": "ACS Omega",
      "doi": "10.1021/acsomega.5c04764",
      "pmid": null,
      "published_date": "2025 Aug 01"
    },
    "status": "released",
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          "long_name": "Ribosome maturation protein SBDS",
          "short_name": "SBDS",
          "sequence": "MSIFTPTNQIRLTNVAVVRMKRAGKRFEIACYKNKVVGWRSGVEKDLDEVLQTHSVFVNVSKGQVAKKEDLISAFGTDDQTEICKQILTKGEVQVSDKERHTQLEQMFRDIATIVADKCVNPETKRPYTVILIERAMKDIHYSVKTNKSTKQQALEVIKQLKEKMKIERAHMRLRFILPVNEGKKLKEKLKPLIKVIESEDYGQQLEIVCLIDPGCFREIDELIKKETKGKGSLEVLNLKDVEEGDEKFE",
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          "uniprot_code": "Q9Y3A5",
          "uniprot_range_first": 1,
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View the complete manifest.json source
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