SASDB55

Glycosylated myelin-associated glycoprotein full extracellular domain (immunoglobulin domains 1-5)

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2019-12-06T13:07:15.624532+01:00

The model fit displayed in this entry represents the volume fraction weighted contributions of the myelin-associated glycoprotein monomer and dimer structures (determined from X-ray crystallography) present in the sample.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Glycosylated myelin-associated glycoprotein full extracellular domain (immunoglobulin domains 1-5)

Concentration— – 3.38 mg/mlBuffer / pH25 mM HEPES 150 mM NaCl / 7.5
Experimental temperature20.0 Facility / beamlineESRF / BM29
Wavelength0.93 nmExposure2.0 s × 9

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Myelin-associated glycoprotein Ig domains 1-5
View sequence
GHWGAWMPSTISAFEGTCVSIPCRFDFPDELRPAVVHGVWYFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGDLGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGLGEPTVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPPVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGMVLREAVAKSLYLDLEEVTPGEDGVYACLAENAYGQDNRTVELSVMYAPWKPTVNGTVVAVEGETVSILCSTQSNPDPILTIFKEKQILATVIYESQLQLELPAVTPEDDGEYWCVAENQYGQRATAFNLSVEFAPIILLESHCAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNETEREFVYSERSGLLLTSILTIRGQAQAPPRVICTSRNLYGTQSLELPFQGAHR
proteinMus musculusP2091720–508dimerMolecule count 253.963 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11043[3]0.0363402–4.969332 1/nmHas uncertainty columnMissing 01sasbdb/entries/55/sasdb55/source/SASDB55.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)23.79—nm
i0Guinier76.790.098—
i0P(r)76.610.08—
mwExperimental77.0—kDa
porod_volumePorod177.0—nm³
rgGuinier6.80.22nm
rgP(r)6.990.009nm

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 name25 mM HEPES 150 mM NaClBuffer concentration25.0 mM
pH7.5Additives150 mM NaCl
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2014-09-11Storage / measurement temperature20.0 / 20.0
Exposure time2.0Frames9
Wavelength0.93Sample-to-detector distance2.43
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineESRF / BM29 · Grenoble, France
q range0.036 – 4.969Sample 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:169 field values
Field pathRaw value
codeSASDB55
statusPublished
type_of_curveSingle concentration
angular_unit1/nm
project.titleStructural basis of myelin-associated glycoprotein adhesion and signalling.
project.publication.titleStructural basis of myelin-associated glycoprotein adhesion and signalling.
project.publication.author_listPronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ
project.publication.journalNat Commun
project.publication.doi10.1038/ncomms13584
project.publication.pmid27922006
project.publication.published_date2016 Dec 6
project.statusreleased
project.submitted_date2016-07-24
project.released_date2016-12-13
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experiment.instrument.detector.typeDectris
experiment.instrument.detector.namePilatus 1M
experiment.instrument.detector.resolution172.0
experiment.instrument.nameESRF
experiment.instrument.cityGrenoble
experiment.instrument.countryFrance
experiment.instrument.beamline_nameBM29
experiment.instrument.beam_geometry
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_nameMyelin-associated glycoprotein Ig domains 1-5
experiment.sample.molecule[0].short_nameMAG
experiment.sample.molecule[0].sequenceGHWGAWMPSTI SAFEGTCVSI PCRFDFPDEL RPAVVHGVWY FNSPYPKNYP PVVFKSRTQV VHESFQGRSR LLGDLGLRNC TLLLSTLSPE LGGKYYFRGD LGGYNQYTFS EHSVLDIVNT PNIVVPPEVV AGTEVEVSCM VPDNCPELRP ELSWLGHEGL GEPTVLGRLR EDEGTWVQVS LLHFVPTREA NGHRLGCQAA FPNTTLQFEG YASLDVKYPP VIVEMNSSVE AIEGSHVSLL CGADSNPPPL LTWMRDGMVL REAVAKSLYL DLEEVTPGED GVYACLAENA YGQDNRTVEL SVMYAPWKPT VNGTVVAVEG ETVSILCSTQ SNPDPILTIF KEKQILATVI YESQLQLELP AVTPEDDGEY WCVAENQYGQ RATAFNLSVE FAPIILLESH CAAARDTVQC LCVVKSNPEP SVAFELPSRN VTVNETEREF VYSERSGLLL TSILTIRGQA QAPPRVICTS RNLYGTQSLE LPFQGAHR
experiment.sample.molecule[0].organismMus musculus
experiment.sample.molecule[0].uniprot_codeP20917
experiment.sample.molecule[0].uniprot_range_first20
experiment.sample.molecule[0].uniprot_range_last508
experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMIFLATLPLFWIMISASRGGHWGAWMPSTISAFEGTCVSIPCRFDFPDELRPAVVHGVWY FNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGD LGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGL GEPTVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPP VIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGMVLREAVAKSLYLDLEEVTPGED GVYACLAENAYGQDNRTVELSVMYAPWKPTVNGTVVAVEGETVSILCSTQSNPDPILTIF KEKQILATVIYESQLQLELPAVTPEDDGEYWCVAENQYGQRATAFNLSVEFAPIILLESH CAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNETEREFVYSERSGLLLTSILTIRGQA QAPPRVICTSRNLYGTQSLELPFQGAHRLMWAKIGPVGAVVAFAILIAIVCYITQTRRKK NVTESSSFSGGDNPHVLYSPEFRISGAPDKYESEKQRLGSERRLLGLRGESPELDLSYSH SDLGKRPTKDSYTLTEELAEYAEIRVK
experiment.sample.molecule[0].mw53.963
experiment.sample.molecule[0].total_mw107.927
experiment.sample.molecule[0].number_molecules2
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.name25 mM HEPES 150 mM NaCl
experiment.sample.buffer.concentration_unitmM
experiment.sample.buffer.commentnull
experiment.sample.buffer.additive150 mM NaCl
experiment.sample.buffer.concentration25.0
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameGlycosylated myelin-associated glycoprotein full extracellular domain (immunoglobulin domains 1-5)
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].addressUtrecht, Netherlands
experiment.contributor[0].affiliation[0].full_nameUtrecht University
experiment.contributor[0].affiliation[0].webpagehttp://www.uu.nl/
experiment.contributor[0].contributor_nameMatti
experiment.contributor[0].contributor_surnamePronker
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitmg/ml
experiment.date2014-09-11
experiment.storage_temperature20.0
experiment.cell_temperature20.0
experiment.exposure_time2.0
experiment.number_of_frames9
experiment.wavelength0.93
experiment.sample_detector_distance2.43
experiment.concentration_minnull
experiment.concentration_max3.38
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.036
experiment.s_max4.969
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].chi_square_value16.4
fits[0].p_value0.0
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fits[0].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionnull
i0_calibration_standardnull
descriptionThe model fit displayed in this entry represents the volume fraction weighted contributions of the myelin-associated glycoprotein monomer and dimer structures (determined from X-ray crystallography) present in the sample.
experiment_descriptionX-ray synchrotron radiation scattering data from solutions of myelin-associated glycoprotein in 25 mM HEPES, 150 mM NaCl, pH 7.5 were collected on the BM29 camera on the storage ring ESRF (Grenoble, France) using a 2D Photon counting Pilatus 1M pixel detector (I(s) vs s, where s = 4π sin θ/λ; 2θ is the scattering angle). One solute concentration of 3.38 mg/ml was measured from nine successive 2 second frames. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the different curves were scaled for protein concentration. The low angle data collected were obtained from a single concentration scattering curve.
tags[]
intensity_unitnull
experimental_mw77.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i076.61
pddf_i0_error0.08
guinier_i076.79
guinier_i0_error0.098
pddf_rg6.99
pddf_rg_error0.009
guinier_rg6.8
guinier_rg_error0.22
pddf_dmax23.79
pddf_dmax_errornull
porod_volume177.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first11
guinier_point_last28
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDB55_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDB55
statussuccess
started_at2026-08-11T16:25:33.886494+00:00
finished_at2026-08-11T16:25:43.915204+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDB55",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/nm",
  "project": {
    "title": "Structural basis of myelin-associated glycoprotein adhesion and signalling.",
    "publication": {
      "title": "Structural basis of myelin-associated glycoprotein adhesion and signalling.",
      "author_list": "Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ",
      "journal": "Nat Commun",
      "doi": "10.1038/ncomms13584",
      "pmid": "27922006",
      "published_date": "2016 Dec 6"
    },
    "status": "released",
    "submitted_date": "2016-07-24",
    "released_date": "2016-12-13"
  },
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      "type_of_source": "X-ray synchrotron",
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    "sample": {
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        {
          "long_name": "Myelin-associated glycoprotein Ig domains 1-5",
          "short_name": "MAG",
          "sequence": "GHWGAWMPSTI SAFEGTCVSI PCRFDFPDEL\r\nRPAVVHGVWY FNSPYPKNYP PVVFKSRTQV VHESFQGRSR LLGDLGLRNC\r\nTLLLSTLSPE LGGKYYFRGD LGGYNQYTFS EHSVLDIVNT PNIVVPPEVV\r\nAGTEVEVSCM VPDNCPELRP ELSWLGHEGL GEPTVLGRLR EDEGTWVQVS\r\nLLHFVPTREA NGHRLGCQAA FPNTTLQFEG YASLDVKYPP VIVEMNSSVE\r\nAIEGSHVSLL CGADSNPPPL LTWMRDGMVL REAVAKSLYL DLEEVTPGED\r\nGVYACLAENA YGQDNRTVEL SVMYAPWKPT VNGTVVAVEG ETVSILCSTQ\r\nSNPDPILTIF KEKQILATVI YESQLQLELP AVTPEDDGEY WCVAENQYGQ\r\nRATAFNLSVE FAPIILLESH CAAARDTVQC LCVVKSNPEP SVAFELPSRN\r\nVTVNETEREF VYSERSGLLL TSILTIRGQA QAPPRVICTS RNLYGTQSLE\r\nLPFQGAHR",
          "organism": "Mus musculus",
          "uniprot_code": "P20917",
          "uniprot_range_first": 20,
          "uniprot_range_last": 508,
          "oligomerization": "dimer",
          "molecular_type": "protein",
          "uniprot_sequence": "MIFLATLPLFWIMISASRGGHWGAWMPSTISAFEGTCVSIPCRFDFPDELRPAVVHGVWY\nFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGD\nLGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGL\nGEPTVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPP\nVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGMVLREAVAKSLYLDLEEVTPGED\nGVYACLAENAYGQDNRTVELSVMYAPWKPTVNGTVVAVEGETVSILCSTQSNPDPILTIF\nKEKQILATVIYESQLQLELPAVTPEDDGEYWCVAENQYGQRATAFNLSVEFAPIILLESH\nCAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNETEREFVYSERSGLLLTSILTIRGQA\nQAPPRVICTSRNLYGTQSLELPFQGAHRLMWAKIGPVGAVVAFAILIAIVCYITQTRRKK\nNVTESSSFSGGDNPHVLYSPEFRISGAPDKYESEKQRLGSERRLLGLRGESPELDLSYSH\nSDLGKRPTKDSYTLTEELAEYAEIRVK",
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          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        }
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        "name": "25 mM HEPES 150 mM NaCl",
        "concentration_unit": "mM",
        "comment": null,
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        "pka": null,
        "ph": 7.5,
        "deuteration": null
      },
      "purity_method": null,
      "name": "Glycosylated myelin-associated glycoprotein full extracellular domain (immunoglobulin domains 1-5)",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": null,
            "address": "Utrecht, Netherlands",
            "full_name": "Utrecht University",
            "webpage": "http://www.uu.nl/"
          }
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        "contributor_name": "Matti",
        "contributor_surname": "Pronker",
        "orcid": null
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    "concentration_method": null,
    "concentration_unit": "mg/ml",
    "date": "2014-09-11",
    "storage_temperature": 20.0,
    "cell_temperature": 20.0,
    "exposure_time": 2.0,
    "number_of_frames": 9,
    "wavelength": 0.93,
    "sample_detector_distance": 2.43,
    "concentration_min": null,
    "concentration_max": 3.38,
    "sample_volume": null,
    "flow_rate": null,
    "s_min": 0.036,
    "s_max": 4.969,
    "total_exposure_time": null,
    "seccolumn": null
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          "software_version": "",
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          "user": 52
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  "description": "The model fit displayed in this entry represents the volume fraction weighted contributions of the myelin-associated glycoprotein monomer and dimer structures (determined from X-ray crystallography) present in the sample.",
  "experiment_description": "X-ray synchrotron radiation scattering data from solutions of myelin-associated glycoprotein in 25 mM HEPES, 150 mM NaCl, pH 7.5 were collected on the BM29 camera on the storage ring ESRF (Grenoble, France) using a 2D Photon counting Pilatus 1M pixel detector (I(s) vs s, where s = 4π sin θ/λ; 2θ is the scattering angle). One solute concentration of 3.38 mg/ml was measured from nine successive 2 second frames. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the different curves were scaled for protein concentration. The low angle data collected were obtained from a single concentration scattering curve.",
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  "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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