SASDGH2

Interleukin 11, N-terminally truncated

Data type: SASBDB experimental data Status: Published Curve type: SEC-SAS Last updated: 2021-04-14T10:05:01.159563+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Interleukin 11, N-terminally truncated

Concentration— – 5.0 Buffer / pH20 mM Tris, 150 mM NaCl, 0.2% sodium azide / 8.5
Experimental temperature20.0 Facility / beamlineAustralian Synchrotron / SAXS/WAXS
Wavelength0.1078 nmExposure1.0 s × 8

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Interleukin 11
View sequence
GSPDPRAELDSTVLLTRSLLADTRQLAAQLRDKFPADGDHNLDSLPTLAMSAGALGALQLPGVLTRLRADLLSYLRHVQWLRRAGGSSLKTLEPELGTLQARLDRLLRRLQLLMSRLALPQPPPDPPAPPLAPPSSAWGGIRAAHAILGGLHLTLDWAVRGLLLLKTRL
proteinHomo sapiensA8K3F732–199monomerMolecule count 118.249 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1672[3]0.007374195–0.6638687 1/AHas uncertainty columnMissing 012sasbdb/entries/h2/sasdgh2/source/SASDGH2.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)5.4—Å
i0Guinier0.0061222.4e-051/cm
i0P(r)0.006139—1/cm
mwExperimental16.3—kDa
mwPorod13.6—kDa
porod_volumePorod21.7—ų
rgGuinier1.7430.011Å
rgP(r)1.76—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 Tris, 150 mM NaCl, 0.2% sodium azideBuffer concentration—
pH8.5Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2019-06-08Storage / measurement temperature— / 20.0
Exposure time1.0Frames8
Wavelength0.1078Sample-to-detector distance2.038
SourceX-ray synchrotronDetectorPilatus3 S 2M
Facility / beamlineAustralian Synchrotron / SAXS/WAXS · Melbourne, Australia
q range0.074 – 6.639Sample volume / flow rate50.0 / 0.45

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:159 field values
Field pathRaw value
codeSASDGH2
statusPublished
type_of_curveSEC-SAS
angular_unit1/A
project.titleThe structure of the extracellular domains of human interleukin 11 α-receptor reveals mechanisms of cytokine engagement
project.publication.titleThe structure of the extracellular domains of human interleukin 11 α-receptor reveals mechanisms of cytokine engagement
project.publication.author_listMetcalfe R, Aizel K, Zlatic C, Nguyen P, Morton C, Lio D, Cheng H, Dobson R, Parker M, Gooley P, Putoczki T, Griffin M
project.publication.journalJournal of Biological Chemistry
project.publication.doi10.1074/jbc.RA119.012351
project.publication.pmidnull
project.publication.published_date2020 Apr 24
project.statusreleased
project.submitted_date2019-07-24
project.released_date2020-04-25
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experiment.instrument.detector.resolution172.0
experiment.instrument.nameAustralian Synchrotron
experiment.instrument.cityMelbourne
experiment.instrument.countryAustralia
experiment.instrument.beamline_nameSAXS/WAXS
experiment.instrument.beam_geometrynull
experiment.instrument.type_of_sourceX-ray synchrotron
experiment.instrument.point_sourcenull
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experiment.instrument.beam_profile_ahnull
experiment.instrument.beam_profile_alnull
experiment.sample.molecule[0].long_nameInterleukin 11
experiment.sample.molecule[0].short_nameIL11
experiment.sample.molecule[0].sequenceGSPDPRAELDSTVLLTRSLLADTRQLAAQLRDKFPADGDHNLDSLPTLAMSAGALGALQLPGVLTRLRADLLSYLRHVQWLRRAGGSSLKTLEPELGTLQARLDRLLRRLQLLMSRLALPQPPPDPPAPPLAPPSSAWGGIRAAHAILGGLHLTLDWAVRGLLLLKTRL
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeA8K3F7
experiment.sample.molecule[0].uniprot_range_first32
experiment.sample.molecule[0].uniprot_range_last199
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMNCVCRLVLVVLSLWPDTAVAPGPPPGPPRVSPDPRAELDSTVLLTRSLLADTRQLAAQL RDKFPADGDHNLDSLPTLAMSAGALGALQLPGVLTRLRADLLSYLRHVQWLRRAGGSSLK TLEPELGTLQARLDRLLRRLQLLMSRLALPQPPPDPPAPPLAPPSSAWGGIRAAHAILGG LHLTLDWAVRGLLLLKTRL
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experiment.sample.molecule[0].total_mw18.249
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experiment.sample.molecule[0].deuterationnull
experiment.sample.molecule[0].molecule_sourcebiological
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experiment.sample.buffer.name20 mM Tris, 150 mM NaCl, 0.2% sodium azide
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
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experiment.sample.buffer.pkanull
experiment.sample.buffer.ph8.5
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experiment.sample.purity_methodnull
experiment.sample.nameInterleukin 11, N-terminally truncated
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].addressMelbourne, Australia
experiment.contributor[0].affiliation[0].full_nameBio21 Institute, The University of Melbourne
experiment.contributor[0].affiliation[0].webpagehttp://www.bio21.unimelb.edu.au/
experiment.contributor[0].contributor_nameRiley D.
experiment.contributor[0].contributor_surnameMetcalfe
experiment.contributor[0].orcidhttps://orcid.org/0000-0002-7154-780X
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2019-06-08
experiment.storage_temperaturenull
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experiment.exposure_time1.0
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experiment.wavelength0.1078
experiment.sample_detector_distance2.038
experiment.concentration_minnull
experiment.concentration_max5.0
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experiment.total_exposure_timenull
experiment.seccolumn2
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fits[0].models[0].pdb_link[0].pdb_code6o4o
fits[0].models[0].pdb_link[0].ext_code6O4O
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pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from solutions of N-terminally truncated interleukin 11 in 20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH 8.5 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Dectris/Pilatus3 S 2M detector at a sample-detector distance of 2.0 m and at a wavelength of λ = 0.1078 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 0.45 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. Eight successive 1 second frames were collected through the SEC elution peak of the sample. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
tags[]
intensity_unit1/cm
experimental_mw16.3
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw13.6
porod_mw_errornull
pddf_i00.006139
pddf_i0_errornull
guinier_i00.006122
guinier_i0_error2.4e-05
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pddf_rg_errornull
guinier_rg1.743
guinier_rg_error0.011
pddf_dmax5.4
pddf_dmax_errornull
porod_volume21.7
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first4
guinier_point_last70
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDGH2_datloglog_img.png
symmetrynull
last_modified2021-04-14T10:05:01.159563+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDGH2
statussuccess
started_at2026-08-11T13:38:49.897099+00:00
finished_at2026-08-11T13:38:58.681326+00:00
source_last_modified2021-04-14T10:05:01.159563+02:00
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View the complete summary.json source
{
  "code": "SASDGH2",
  "status": "Published",
  "type_of_curve": "SEC-SAS",
  "angular_unit": "1/A",
  "project": {
    "title": "The structure of the extracellular domains of human interleukin 11 α-receptor reveals mechanisms of cytokine engagement",
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      "author_list": "Metcalfe R, Aizel K, Zlatic C, Nguyen P, Morton C, Lio D, Cheng H, Dobson R, Parker M, Gooley P, Putoczki T, Griffin M",
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      "pmid": null,
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View the complete manifest.json source
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