SASDGC6

Glucuronoyl esterase, deglycolsylated full length

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2020-11-03T10:09:09.624639+01:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Glucuronoyl esterase, deglycolsylated full length

Concentration— – 3.7 Buffer / pH20 mM sodium acetate / 5.0
Experimental temperature21.0 Facility / beamlineUniversity of Copenhagen, Department of Drug Design and Pharmacology / Xenocs BioXolver L with GeniX3D
Wavelength0.154 nmExposure60.0 s × 10

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
4-O-methyl-glucuronoyl methylesterase (Glucuronoyl esterase)
View sequence
>FL_CUGE/1-481MQASAPQWGQCGGIGWTGPTACPSGWACQQLNAYYSQCLQGAAPAPARTTAAPPPPPATTAAPPPPTTSAPTGSSPVAGACGAIASTVPNYNNAKLPDPFTFANGTALRTKADWSCRRAEISALIQNYEAGTLPPKPPVVTASFSKSGNTGTLAITAGLSNSQTIKFSPTISYPSGTPPANGWPLIIAYEGGSIPIPAGVATLTYSNSDMAQQNSASSRGQGLFYQLYGSTHSASAMTAWVWGVSRIIDALEMTPTAQINTQRIGVTGCSRDGKGALMAGAFEERIALTIPQESGSGGDACWRLSKYEIDNGNQVQDAVEIVGENVWFSTNFNNYVQKLPTVPEDHHLLAAMVAPRAMISFENTDYLWLSPMSSFGCMTAAHTVWQGLGIADSHGFAQVGGHAHCAWPSSLTPQLNAFINRFLLDQSATTNVFTTNNQFGKVQWNAANWITWTTPTLTGLEQKLISEEDLNSAVDHHHHHH
proteinCerrena unicolorA0A0A7EQR318–474monomerMolecule count 150.907 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1378[3]0.01966381–0.480481 1/AHas uncertainty columnMissing 024sasbdb/entries/c6/sasdgc6/source/SASDGC6.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)11.0—Å
i0Guinier0.0620.00093arbitrary
i0P(r)0.05964—arbitrary
mwExperimental45.0—kDa
mwPorod44.0—kDa
porod_volumePorod71.0—ų
rgGuinier3.190.29Å
rgP(r)3.19—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 name20 mM sodium acetateBuffer concentration—
pH5.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2018-10-10Storage / measurement temperature21.0 / 21.0
Exposure time60.0Frames10
Wavelength0.154Sample-to-detector distance0.571
SourceX-ray in houseDetectorPilatus3 R 300K
Facility / beamlineUniversity of Copenhagen, Department of Drug Design and Pharmacology / Xenocs BioXolver L with GeniX3D · Copenhagen, Denmark
q range0.197 – 4.805Sample 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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All source fields (unfiltered)

Every source field is expanded here, including empty values, list members and fields already shown above.

summary.json:179 field values
Field pathRaw value
codeSASDGC6
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleThe structural basis of fungal glucuronoyl esterase activity on natural substrates.
project.publication.titleThe structural basis of fungal glucuronoyl esterase activity on natural substrates.
project.publication.author_listErnst HA, Mosbech C, Langkilde AE, Westh P, Meyer AS, Agger JW, Larsen S
project.publication.journalNat Commun
project.publication.doi10.1038/s41467-020-14833-9
project.publication.pmid32094331
project.publication.published_date2020 Feb 24
project.statusreleased
project.submitted_date2019-09-27
project.released_date2020-02-28
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experiment.instrument.detector.typepixel counting
experiment.instrument.detector.namePilatus3 R 300K
experiment.instrument.detector.resolution172.0
experiment.instrument.nameUniversity of Copenhagen, Department of Drug Design and Pharmacology
experiment.instrument.cityCopenhagen
experiment.instrument.countryDenmark
experiment.instrument.beamline_nameXenocs BioXolver L with GeniX3D
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_name4-O-methyl-glucuronoyl methylesterase (Glucuronoyl esterase)
experiment.sample.molecule[0].short_nameCuGE
experiment.sample.molecule[0].sequence>FL_CuGE/1-481 MQASAPQWGQCGGIGWTGPTACPSGWACQQLNAYYSQCLQGAAPAPARTTAAPPPPPATTAAPPPPTTSAPT GSSPVAGACGAIASTVPNYNNAKLPDPFTFANGTALRTKADWSCRRAEISALIQNYEAGTLPPKPPVVTASF SKSGNTGTLAITAGLSNSQTIKFSPTISYPSGTPPANGWPLIIAYEGGSIPIPAGVATLTYSNSDMAQQNSA SSRGQGLFYQLYGSTHSASAMTAWVWGVSRIIDALEMTPTAQINTQRIGVTGCSRDGKGALMAGAFEERIAL TIPQESGSGGDACWRLSKYEIDNGNQVQDAVEIVGENVWFSTNFNNYVQKLPTVPEDHHLLAAMVAPRAMIS FENTDYLWLSPMSSFGCMTAAHTVWQGLGIADSHGFAQVGGHAHCAWPSSLTPQLNAFINRFLLDQSATTNV FTTNNQFGKVQWNAANWITWTTPTLTGLEQKLISEEDLNSAVDHHHHHH
experiment.sample.molecule[0].organismCerrena unicolor
experiment.sample.molecule[0].uniprot_codeA0A0A7EQR3
experiment.sample.molecule[0].uniprot_range_first18
experiment.sample.molecule[0].uniprot_range_last474
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMFKPSFVALALVSYATAQASAPQWGQCGGIGWTGPTACPSGWACQQLNAYYSQCLQGAAP APARTTAAPPPPPATTAAPPPPTTSAPTGSSPVAGACGAIASTVPNYNNAKLPDPFTFAN GTALRTKADWSCRRAEISALIQNYEAGTLPPKPPVVTASFSKSGNTGTLAITAGLSNSQT IKFSPTISYPSGTPPANGWPLIIAYEGGSIPIPAGVATLTYSNSDMAQQNSASSRGQGLF YQLYGSTHSASAMTAWVWGVSRIIDALEMTPTAQINTQRIGVTGCSRDGKGALMAGAFEE RIALTIPQESGSGGDACWRLSKYEIDNGNQVQDAVEIVGENVWFSTNFNNYVQKLPTVPE DHHLLAAMVAPRAMISFENTDYLWLSPMSSFGCMTAAHTVWQGLGIADSHGFAQVGGHAH CAWPSSLTPQLNAFINRFLLDQSATTNVFTTNNQFGKVQWNAANWITWTTPTLT
experiment.sample.molecule[0].mw50.907
experiment.sample.molecule[0].total_mw50.907
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.name20 mM sodium acetate
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph5.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameGlucuronoyl esterase, deglycolsylated full length
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].addressCopenhagen, Denmark
experiment.contributor[0].affiliation[0].full_nameUniversity of Copenhagen
experiment.contributor[0].affiliation[0].webpagehttp://www.ku.dk/
experiment.contributor[0].contributor_nameAnnette
experiment.contributor[0].contributor_surnameLangkilde
experiment.contributor[0].orcid
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2018-10-10
experiment.storage_temperature21.0
experiment.cell_temperature21.0
experiment.exposure_time60.0
experiment.number_of_frames10
experiment.wavelength0.154
experiment.sample_detector_distance0.571
experiment.concentration_minnull
experiment.concentration_max3.7
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.197
experiment.s_max4.805
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[1].description
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionSAXS data from solutions of full-length deglycolsylated glucuronoyl esterase in 20 mM sodium acetate, pH 5 were collected using a Xenocs BioXolver L with GeniX3D (University of Copenhagen, Department of Drug Design and Pharmacology) equipped with a Pilatus3 R 300K detector at a sample-detector distance of 0.6 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.70 mg/ml was measured at 21°C. 10 successive 60 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_mw45.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw44.0
porod_mw_errornull
pddf_i00.05964
pddf_i0_errornull
guinier_i00.062
guinier_i0_error0.00093
pddf_rg3.19
pddf_rg_errornull
guinier_rg3.19
guinier_rg_error0.29
pddf_dmax11.0
pddf_dmax_errornull
porod_volume71.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first2
guinier_point_last18
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDGC6_datloglog_img.png
symmetrynull
last_modified2020-11-03T10:09:09.624639+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDGC6
statussuccess
started_at2026-08-11T15:06:16.945258+00:00
finished_at2026-08-11T15:06:25.265098+00:00
source_last_modified2020-11-03T10:09:09.624639+01:00
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View the complete summary.json source
{
  "code": "SASDGC6",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "The structural basis of fungal glucuronoyl esterase activity on natural substrates.",
    "publication": {
      "title": "The structural basis of fungal glucuronoyl esterase activity on natural substrates.",
      "author_list": "Ernst HA, Mosbech C, Langkilde AE, Westh P, Meyer AS, Agger JW, Larsen S",
      "journal": "Nat Commun",
      "doi": "10.1038/s41467-020-14833-9",
      "pmid": "32094331",
      "published_date": "2020 Feb 24"
    },
    "status": "released",
    "submitted_date": "2019-09-27",
    "released_date": "2020-02-28"
  },
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      "city": "Copenhagen",
      "country": "Denmark",
      "beamline_name": "Xenocs BioXolver L with GeniX3D",
      "beam_geometry": null,
      "type_of_source": "X-ray in house",
      "point_source": null,
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          "uniprot_range_last": 474,
          "oligomerization": "monomer",
          "molecular_type": "protein",
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          "molecule_source": "biological",
          "molecule_description": null
        }
      ],
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      "ext_coefficient": null,
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      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
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        "affiliation": [
          {
            "short_name": null,
            "address": "Copenhagen, Denmark",
            "full_name": "University of Copenhagen",
            "webpage": "http://www.ku.dk/"
          }
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        "contributor_name": "Annette",
        "contributor_surname": "Langkilde",
        "orcid": ""
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    "concentration_unit": null,
    "date": "2018-10-10",
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    "flow_rate": null,
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View the complete manifest.json source
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