SASDD53

Tetratrico peptide repeat domain of Bacterial cellulose synthesis subunit C

Data type: SASBDB experimental data Status: Published Curve type: Extrapolated to infinite dilution Last updated: 2019-12-06T13:07:15.624532+01:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Tetratrico peptide repeat domain of Bacterial cellulose synthesis subunit C

Concentration0.71 – 1.8 Buffer / pH50 mM HEPES, 100 mM KCl / 8.0
Experimental temperature20.0 Facility / beamlinePhoton Factory (PF), High Energy Accelerator Research Organization (KEK) / BL-10C
Wavelength0.1 nmExposure20.0 s × 28

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Bacterial cellulose synthesis subunit C
View sequence
GHMDEPTAQQQLLSQVRLGEATKREDLVRQSLYRLELIDPDNPDVIAARFRYLLRQGDNAGAQKQLDRMKQLAPDSAAYKSSVTSMTLSGAEGRQALQQARLQATTGHVPEALAAYDALFKGNPPEGDLAVEYWALVAKVPARRSEAITQLKALNARNPGNAALQNSLAQLLFGEGRDAEAYAVLEQMAKSSAGREAAAGLWYQQIQRMPVSDASVKALQRFLTVFSSGDTVDSARTQLAAQQKQLADPAFRARATGLAAVDAGQGAKAVNELRQAVNANGTDSEAVGALGQAYSQSGDRARAVAQFEKAIAMDPTSGNRSKWDSLLKTNRYWLLIQQGDAALKANNPGEAERLYSQARRIDNTDSYAVLGLGDAAMARKDSHAAESFYRQALRMDSGNSNAVRGLANIYRARSPQEADTFIQSLSASQRRSIDDIERGLKNDRLAQQAEALENSGQWAQAAELQRQRLALDPGSVWVTYRLASDLRQAGEPREADAHMQRLAALKPGDPEQVYAYGLYLSGNNQEMAALNQLNALPKAQWNSNIQELAERLQTNRLLDNANRLRDSGHEEQARALLAQQPASTRIDLTLADWAQQGGDSASAQHYFNRVLEREPNNQDALLGLAELYAADGNKMAARAQLAKLLEHHHHHH
proteinEnterobacter sp. CJF-002K0J1W824–664monomerMolecule count 171.298 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11461[3]0.008331668–0.400117 1/AHas uncertainty columnMissing 00sasbdb/entries/53/sasdd53/source/SASDD53.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)18.53—Å
i0Guinier0.1050.00041/cm
i0P(r)0.10350.00031/cm
mwExperimental73.4—kDa
mwGuinier I(0)73.40.5kDa
mwPorod72.1—kDa
porod_volumePorod115.3—ų
rgGuinier5.120.08Å
rgP(r)5.130.02Å

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 HEPES, 100 mM KClBuffer concentration—
pH8.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2017-04-24Storage / measurement temperature20.0 / 20.0
Exposure time20.0Frames28
Wavelength0.1Sample-to-detector distance2.01
SourceX-ray synchrotronDetectorPilatus3 2M
Facility / beamlinePhoton Factory (PF), High Energy Accelerator Research Organization (KEK) / BL-10C · Tsukuba, Japan
q range0.083 – 4.001Sample 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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full_entry_zip:source record and ZIP contents (4 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:156 field values
Field pathRaw value
codeSASDD53
statusPublished
type_of_curveExtrapolated to infinite dilution
angular_unit1/A
project.titleCrystal structure of the flexible tandem repeat domain of bacterial cellulose synthesis subunit C.
project.publication.titleCrystal structure of the flexible tandem repeat domain of bacterial cellulose synthesis subunit C.
project.publication.author_listNojima S, Fujishima A, Kato K, Ohuchi K, Shimizu N, Yonezawa K, Tajima K, Yao M
project.publication.journalSci Rep
project.publication.doi10.1038/s41598-017-12530-0
project.publication.pmid29026093
project.publication.published_date2017 Oct 12
project.statusreleased
project.submitted_date2018-01-17
project.released_date2018-01-17
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experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus3 2M
experiment.instrument.detector.resolution0.172
experiment.instrument.namePhoton Factory (PF), High Energy Accelerator Research Organization (KEK)
experiment.instrument.cityTsukuba
experiment.instrument.countryJapan
experiment.instrument.beamline_nameBL-10C
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_nameBacterial cellulose synthesis subunit C
experiment.sample.molecule[0].short_nameBcsC-TPR
experiment.sample.molecule[0].sequenceGHMDEPTAQQQLLSQVRLGEATKREDLVRQSLYRLELIDPDNPDVIAARFRYLLRQGDNAGAQKQLDRMKQLAPDSAAYKSSVTSMTLSGAEGRQALQQARLQATTGHVPEALAAYDALFKGNPPEGDLAVEYWALVAKVPARRSEAITQLKALNARNPGNAALQNSLAQLLFGEGRDAEAYAVLEQMAKSSAGREAAAGLWYQQIQRMPVSDASVKALQRFLTVFSSGDTVDSARTQLAAQQKQLADPAFRARATGLAAVDAGQGAKAVNELRQAVNANGTDSEAVGALGQAYSQSGDRARAVAQFEKAIAMDPTSGNRSKWDSLLKTNRYWLLIQQGDAALKANNPGEAERLYSQARRIDNTDSYAVLGLGDAAMARKDSHAAESFYRQALRMDSGNSNAVRGLANIYRARSPQEADTFIQSLSASQRRSIDDIERGLKNDRLAQQAEALENSGQWAQAAELQRQRLALDPGSVWVTYRLASDLRQAGEPREADAHMQRLAALKPGDPEQVYAYGLYLSGNNQEMAALNQLNALPKAQWNSNIQELAERLQTNRLLDNANRLRDSGHEEQARALLAQQPASTRIDLTLADWAQQGGDSASAQHYFNRVLEREPNNQDALLGLAELYAADGNKMAARAQLAKLLEHHHHHH
experiment.sample.molecule[0].organismEnterobacter sp. CJF-002
experiment.sample.molecule[0].uniprot_codeK0J1W8
experiment.sample.molecule[0].uniprot_range_first24
experiment.sample.molecule[0].uniprot_range_last664
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMRKFTVSLLCLSLVLALTPATQADEPTAQQQLLSQVRLGEATKREDLVRQSLYRLELIDP DNPDVIAARFRYLLRQGDNAGAQKQLDRMKQLAPDSAAYKSSVTSMTLSGAEGRQALQQA RLQATTGHVPEALAAYDALFKGNPPEGDLAVEYWALVAKVPARRSEAITQLKALNARNPG NAALQNSLAQLLFGEGRDAEAYAVLEQMAKSSAGREAAAGLWYQQIQRMPVSDASVKALQ RFLTVFSSGDTVDSARTQLAAQQKQLADPAFRARATGLAAVDAGQGAKAVNELRQAVNAN GTDSEAVGALGQAYSQSGDRARAVAQFEKAIAMDPTSGNRSKWDSLLKTNRYWLLIQQGD AALKANNPGEAERLYSQARRIDNTDSYAVLGLGDAAMARKDSHAAESFYRQALRMDSGNS NAVRGLANIYRARSPQEADTFIQSLSASQRRSIDDIERGLKNDRLAQQAEALENSGQWAQ AAELQRQRLALDPGSVWVTYRLASDLRQAGEPREADAHMQRLAALKPGDPEQVYAYGLYL SGNNQEMAALNQLNALPKAQWNSNIQELAERLQTNRLLDNANRLRDSGHEEQARALLAQQ PASTRIDLTLADWAQQGGDSASAQHYFNRVLEREPNNQDALLGLAELYAADGNKMAARAQ LAKLPAPTAAQPQSINTQRRLALVQAALGDTDSARQTFSRIMPQAKAQPPSMESALVLRD AARFQAQQGEPQQALETWKDAMVASGVTTTPPADNDTFTRLTRNNAKDDWLKRGIRSDAA DLYRQQDINVTLQHDYWGSSGTGGYSDLKAHTTLVQADAPLADGRMFFRTDVVNMNVGSF DTTDDVYDPNWGTCSATPCRGNTSQKANGASLAVGWQNGTWSGDIGTTPMGFDVVDVVGG LSYSSDLGPLGYTVNVHRRPISSSLLAFGGQKDPNTGVTWGGVRATGGGVSLSYDKGEAN GVWSSLNADSLTGKNVADNWRIRWMTGYYYKLINKDNERLTVGLNNMLWHYDKDLSDYTL GQGGYYSPQQYISFAVPVVWRKRTANWSWELGASGSWSHSKTDGIKRYPLQNLIPDNQFF ANGDRMFLDKDNSSTSSSSNGFGYTARALVERRVTSHWFVGAGVDIQQAKDYTPSHALIY VRYSGAGWQGDMDMPPQTLTPYADW
experiment.sample.molecule[0].mw71.298
experiment.sample.molecule[0].total_mw71.298
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.name50 mM HEPES, 100 mM KCl
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.nameTetratrico peptide repeat domain of Bacterial cellulose synthesis subunit C
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_nameKEK
experiment.contributor[0].affiliation[0].addressTsukuba, Japan
experiment.contributor[0].affiliation[0].full_nameHigh Energy Accelerater Research Organization (KEK)
experiment.contributor[0].affiliation[0].webpagehttps://www.kek.jp
experiment.contributor[0].contributor_nameKento
experiment.contributor[0].contributor_surnameYonezawa
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2017-04-24
experiment.storage_temperature20.0
experiment.cell_temperature20.0
experiment.exposure_time20.0
experiment.number_of_frames28
experiment.wavelength0.1
experiment.sample_detector_distance2.01
experiment.concentration_min0.71
experiment.concentration_max1.8
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.083
experiment.s_max4.001
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].softwareDAMMIF
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fits[0].models[0].model_titlenull
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fits[0].models[0].symmetryP1
fits[0].models[0].commentnull
fits[0].models[0].user275
fits[0].fit_unit1/A
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fits[0].softwareDAMMIF
fits[0].chi_square_value1.906
fits[0].p_value0.000126
fits[0].fit_residual_plotSASDD53_fit1_fitresiduals_img.png
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fits[0].software_versionATSAS 2.7
fits[0].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from solutions of Tetratrico peptide repeat domain of Bacterial cellulose synthesis subunit C in 50 mM HEPES, 100 mM KCl, pH 8 were collected on the beam line BL-10C at the Phton Factory (PF; Tsukuba, Ibaraki, Japan) using a Pilatus3 2M detector at a sample-detector distance of 2.01 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle).120 successive 20 second frames were collected at 20°C using size-exclusion chromatography SAXS. Sample was loaded to Superdex 200 increase 10/300 (GE healthcare). The flow rate was set at 0.05 mL/min. The data were normalized to the intensity of the incident beam and circularly averaged; the scattering of the solvent-blank was subtracted. Every five SAXS profiles were averaged to improve the signal-to-noise ratio of the data, and the extrapolated scattering profile at a concentration of zero was calculated with the data in the descent side of the peak (frames 91–118) by ALMERGE of ATSAS. In order to estimate the molecular mass from I(0), the partial specific volume, PSV, (0.7405 cm3/g) and the X-ray scattering contrast (Δρ = 2.949×10^10 cm-2) of this protein were calculated by using the PSV calculator of NucProt (http://www.molmovdb.org/cgi-bin/psv.cgi; Voss & Gerstein (2005) J. Mol. Biol. 346, 477–492) and the contrast module of MULCh (http://smb-research.smb.usyd.edu.au/NCVWeb/input.jsp; Whitten, et al., (2008) J. App. Crystallogr. 41, 222–226).
tags[]
intensity_unit1/cm
experimental_mw73.4
experimental_mw_errornull
guinier_i0_mw73.4
guinier_i0_mw_error0.5
porod_mw72.1
porod_mw_errornull
pddf_i00.1035
pddf_i0_error0.0003
guinier_i00.105
guinier_i0_error0.0004
pddf_rg5.13
pddf_rg_error0.02
guinier_rg5.12
guinier_rg_error0.08
pddf_dmax18.53
pddf_dmax_errornull
porod_volume115.3
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first2
guinier_point_last59
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDD53_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDD53
statussuccess
started_at2026-08-11T13:52:39.941840+00:00
finished_at2026-08-11T13:52:49.578841+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDD53",
  "status": "Published",
  "type_of_curve": "Extrapolated to infinite dilution",
  "angular_unit": "1/A",
  "project": {
    "title": "Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthesis subunit C.",
    "publication": {
      "title": "Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthesis subunit C.",
      "author_list": "Nojima S, Fujishima A, Kato K, Ohuchi K, Shimizu N, Yonezawa K, Tajima K, Yao M",
      "journal": "Sci Rep",
      "doi": "10.1038/s41598-017-12530-0",
      "pmid": "29026093",
      "published_date": "2017 Oct 12"
    },
    "status": "released",
    "submitted_date": "2018-01-17",
    "released_date": "2018-01-17"
  },
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        "type": null,
        "name": "Pilatus3 2M",
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      "name": "Photon Factory (PF), High Energy Accelerator Research Organization (KEK)",
      "city": "Tsukuba",
      "country": "Japan",
      "beamline_name": "BL-10C",
      "beam_geometry": null,
      "type_of_source": "X-ray synchrotron",
      "point_source": null,
      "line_collimation": null,
      "sample_path_length": null,
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      "line_collimation_integrationwidth": null,
      "xray_energy": null,
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      "beam_profile_al": null
    },
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        {
          "long_name": "Bacterial cellulose synthesis subunit C",
          "short_name": "BcsC-TPR",
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          "organism": "Enterobacter sp. CJF-002",
          "uniprot_code": "K0J1W8",
          "uniprot_range_first": 24,
          "uniprot_range_last": 664,
          "oligomerization": "monomer",
          "molecular_type": "protein",
          "uniprot_sequence": "MRKFTVSLLCLSLVLALTPATQADEPTAQQQLLSQVRLGEATKREDLVRQSLYRLELIDP\nDNPDVIAARFRYLLRQGDNAGAQKQLDRMKQLAPDSAAYKSSVTSMTLSGAEGRQALQQA\nRLQATTGHVPEALAAYDALFKGNPPEGDLAVEYWALVAKVPARRSEAITQLKALNARNPG\nNAALQNSLAQLLFGEGRDAEAYAVLEQMAKSSAGREAAAGLWYQQIQRMPVSDASVKALQ\nRFLTVFSSGDTVDSARTQLAAQQKQLADPAFRARATGLAAVDAGQGAKAVNELRQAVNAN\nGTDSEAVGALGQAYSQSGDRARAVAQFEKAIAMDPTSGNRSKWDSLLKTNRYWLLIQQGD\nAALKANNPGEAERLYSQARRIDNTDSYAVLGLGDAAMARKDSHAAESFYRQALRMDSGNS\nNAVRGLANIYRARSPQEADTFIQSLSASQRRSIDDIERGLKNDRLAQQAEALENSGQWAQ\nAAELQRQRLALDPGSVWVTYRLASDLRQAGEPREADAHMQRLAALKPGDPEQVYAYGLYL\nSGNNQEMAALNQLNALPKAQWNSNIQELAERLQTNRLLDNANRLRDSGHEEQARALLAQQ\nPASTRIDLTLADWAQQGGDSASAQHYFNRVLEREPNNQDALLGLAELYAADGNKMAARAQ\nLAKLPAPTAAQPQSINTQRRLALVQAALGDTDSARQTFSRIMPQAKAQPPSMESALVLRD\nAARFQAQQGEPQQALETWKDAMVASGVTTTPPADNDTFTRLTRNNAKDDWLKRGIRSDAA\nDLYRQQDINVTLQHDYWGSSGTGGYSDLKAHTTLVQADAPLADGRMFFRTDVVNMNVGSF\nDTTDDVYDPNWGTCSATPCRGNTSQKANGASLAVGWQNGTWSGDIGTTPMGFDVVDVVGG\nLSYSSDLGPLGYTVNVHRRPISSSLLAFGGQKDPNTGVTWGGVRATGGGVSLSYDKGEAN\nGVWSSLNADSLTGKNVADNWRIRWMTGYYYKLINKDNERLTVGLNNMLWHYDKDLSDYTL\nGQGGYYSPQQYISFAVPVVWRKRTANWSWELGASGSWSHSKTDGIKRYPLQNLIPDNQFF\nANGDRMFLDKDNSSTSSSSNGFGYTARALVERRVTSHWFVGAGVDIQQAKDYTPSHALIY\nVRYSGAGWQGDMDMPPQTLTPYADW",
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          "number_molecules": 1,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
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      "buffer": {
        "name": "50 mM HEPES, 100 mM KCl",
        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 8.0,
        "deuteration": null
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      "purity_method": null,
      "name": "Tetratrico peptide repeat domain of Bacterial cellulose synthesis subunit C",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
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    "contributor": [
      {
        "affiliation": [
          {
            "short_name": "KEK",
            "address": "Tsukuba, Japan",
            "full_name": "High Energy Accelerater Research Organization (KEK)",
            "webpage": "https://www.kek.jp"
          }
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        "contributor_name": "Kento",
        "contributor_surname": "Yonezawa",
        "orcid": null
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    "concentration_method": null,
    "concentration_unit": null,
    "date": "2017-04-24",
    "storage_temperature": 20.0,
    "cell_temperature": 20.0,
    "exposure_time": 20.0,
    "number_of_frames": 28,
    "wavelength": 0.1,
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    "concentration_max": 1.8,
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    "flow_rate": null,
    "s_min": 0.083,
    "s_max": 4.001,
    "total_exposure_time": null,
    "seccolumn": null
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    {
      "models": [
        {
          "model_plot": "https://www.sasbdb.org/media/pdb_file/images/SASDD53_fit1_model1_img.png",
          "software": "DAMMIF",
          "pdb_link": [],
          "model_title": null,
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          "comment": null,
          "user": 275
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      "fit_unit": "1/A",
      "fit_plot": "https://www.sasbdb.org/media/fitting_files/scattering_plots/SASDD53_fit1_fit_img.png",
      "software": "DAMMIF",
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      "fit_residual_plot": "SASDD53_fit1_fitresiduals_img.png",
      "fit_data": "https://www.sasbdb.org/media/fitting_files/SASDD53_fit1.fir",
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  "i0_calibration_standard": null,
  "description": null,
  "experiment_description": "Synchrotron SAXS data from solutions of Tetratrico peptide repeat domain of Bacterial cellulose synthesis subunit C in 50 mM HEPES, 100 mM KCl, pH 8 were collected on the beam line BL-10C at the Phton Factory (PF; Tsukuba, Ibaraki, Japan) using a Pilatus3 2M detector at a sample-detector distance of 2.01 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle).120 successive 20 second frames were collected at 20°C using size-exclusion chromatography SAXS. Sample was loaded to Superdex 200 increase 10/300 (GE healthcare). The flow rate  was set at 0.05 mL/min. The data were normalized to the intensity of the incident beam and circularly averaged; the scattering of the solvent-blank was subtracted. Every five SAXS profiles were averaged to improve the signal-to-noise ratio of the data, and the extrapolated scattering profile at a concentration of zero was calculated with the data in the descent side of the peak (frames 91–118) by ALMERGE of ATSAS. In order to estimate the molecular mass from I(0), the partial specific volume, PSV, (0.7405 cm3/g) and the X-ray scattering contrast (Δρ = 2.949×10^10 cm-2) of this protein were calculated by using the PSV calculator of NucProt (http://www.molmovdb.org/cgi-bin/psv.cgi; Voss & Gerstein (2005) J. Mol. Biol. 346, 477–492) and the contrast module of MULCh (http://smb-research.smb.usyd.edu.au/NCVWeb/input.jsp; Whitten, et al., (2008) J. App. Crystallogr. 41, 222–226).",
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  "intensities_log_log_plot": "SASDD53_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2019-12-06T13:07:15.624532+01:00",
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}
View the complete manifest.json source
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