SASDBG3

Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct)

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

Sample 1 · Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct)

Concentration1.1 – 5.5 Buffer / pH20 mM Tris 150 mM NaCl 3% glycerol / 7.4
Experimental temperature— Facility / beamlineESRF / ID14-3
Wavelength0.09 nmExposure1.0 s × 10

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Mouse Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct)
View sequence
GPMACPPKCRCEKLLFYCDSQGFHSVPNGLPSQLLGLSLRHNQLQSLPNGVFDKLTQLTWLHLDHNQLQSLPNGVFDKLTKLTELILSSNQLQSLPNGTFDKLTNLQNLDLSFNQLQSLPNGVFDKLTNLQTLHLRSNQLQSLPNGVFDKLTSLTFLDLSTNQLQSLPNGVFDKLTNLRELHLEHNQLQSLPNGVFDKLTSLTTLFLQWNQLQSLPNGVFDKLTNLEKLDLTGNQLQSLPNGVFDKLTNLKILLLDNNQLQSLPNGVFDKLKSLTTVGLSGNLWECSPRVCALASWLGSFQGRWEHSILCHSPDHTQGEDILDAVHGFQLCWNLSTTVTAMATTYRDPTTEKLVEKY
proteinMus musculusQ8BGA330–380monomerMolecule count 140.01 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1991[3]0.0785365–4.71044 1/nmHas uncertainty columnMissing 00sasbdb/entries/g3/sasdbg3/source/SASDBG3.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)13.1—nm
i0Guinier59.2——
i0P(r)59.3——
mwExperimental50.0—kDa
mwPorod40.0—kDa
rgGuinier3.31—nm
rgP(r)3.34—nm

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 3% glycerolBuffer concentration20.0 mM
pH7.4Additives150 mM NaCl, 3% glycerol
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2015-09-27Storage / measurement temperature20.0 / —
Exposure time1.0Frames10
Wavelength0.09Sample-to-detector distance2.87
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineESRF / ID14-3 · Grenoble, France
q range0.079 – 4.71Sample 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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pddf:source record
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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
codeSASDBG3
statusPublished
type_of_curveSingle concentration
angular_unit1/nm
project.titleCrystal Structure of an Engineered LRRTM2 Synaptic Adhesion Molecule and a Model for Neurexin Binding.
project.publication.titleCrystal Structure of an Engineered LRRTM2 Synaptic Adhesion Molecule and a Model for Neurexin Binding.
project.publication.author_listPaatero A, Rosti K, Shkumatov AV, Sele C, Brunello C, Kysenius K, Singha P, Jokinen V, Huttunen H, Kajander T
project.publication.journalBiochemistry
project.publication.doi10.1021/acs.biochem.5b00971
project.publication.pmid26785044
project.publication.published_date2016 Feb 16
project.statusreleased
project.submitted_date2016-01-25
project.released_date2016-01-26
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDBG3.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDBG3.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDBG3_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDBG3_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDBG3_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDBG3_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDBG3.sascif
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_nameID14-3
experiment.instrument.beam_geometry
experiment.instrument.type_of_sourceX-ray synchrotron
experiment.instrument.point_sourceTrue
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_nameMouse Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct)
experiment.sample.molecule[0].short_namecLRRTM2 30-380
experiment.sample.molecule[0].sequenceGPMACPPKCRCEKLLFYCDSQGFHSVPNGLPSQLLGLSLRHNQLQSLPNGVFDKLTQLTWLHLDHNQLQSLPNGVFDKLTKLTELILSSNQLQSLPNGTFDKLTNLQNLDLSFNQLQSLPNGVFDKLTNLQTLHLRSNQLQSLPNGVFDKLTSLTFLDLSTNQLQSLPNGVFDKLTNLRELHLEHNQL QSLPNGVFDKLTSLTTLFLQWNQLQSLPNGVFDKLTNLEKLDLTGNQLQSLPNGVFDKLTNLKILLLDNNQLQSLPNGVFDKLKSLTTVGLSGNLWECSPRVCALASWLGSFQGRWEHSILCHSPDHTQGEDILDAVHGFQLCWNLSTTVTAMATTYRDPTTEKLVEKY
experiment.sample.molecule[0].organismMus musculus
experiment.sample.molecule[0].uniprot_codeQ8BGA3
experiment.sample.molecule[0].uniprot_range_first30
experiment.sample.molecule[0].uniprot_range_last380
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMGLHFKWPLGAPMLAAIYAMSVVLKMLPALGMACPPKCRCEKLLFYCDSQGFHSVPNATD KGSLGLSLRHNHITALERDQFASFSQLTWLHLDHNQISTVKEDAFQGLYKLKELILSSNK IFYLPNTTFTQLINLQNLDLSFNQLSSLHPELFYGLRKLQTLHLRSNSLRTIPVRLFWDC RSLEFLDLSTNRLRSLARNGFAGLIKLRELHLEHNQLTKINFAHFLRLSSLHTLFLQWNK ISNLTCGMDWTWSTLEKLDLTGNEIKAIDLTVFETMPNLKILLMDNNKLNSLDSKILNSL KSLTTVGLSGNLWECSPRVCALASWLGSFQGRWEHSILCHSPDHTQGEDILDAVHGFQLC WNLSTTVTAMATTYRDPTTEYTKISSSSYHVGDKEIPTTAGIAVTTEEHFPEPDNAIFTQ RVITGTMALLFSFFFIIFIVFISRKCCPPTLRRIRQCSMIQNHRQLRSQTRLHMSNMSDQ GPYNEYEPTHEGPFIIINGYGQCKCQQLPYKECEV
experiment.sample.molecule[0].mw40.01
experiment.sample.molecule[0].total_mw40.01
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 Tris 150 mM NaCl 3% glycerol
experiment.sample.buffer.concentration_unitmM
experiment.sample.buffer.commentnull
experiment.sample.buffer.additive150 mM NaCl, 3% glycerol
experiment.sample.buffer.concentration20.0
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.4
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameLeucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct)
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_nameVUB
experiment.contributor[0].affiliation[0].addressPleinlaan 2 1050 Brussel
experiment.contributor[0].affiliation[0].full_nameVrije Universiteit Brussel
experiment.contributor[0].affiliation[0].webpagehttp://www.vub.ac.be/
experiment.contributor[0].contributor_nameAlexander
experiment.contributor[0].contributor_surnameShkumatov
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2015-09-27
experiment.storage_temperature20.0
experiment.cell_temperaturenull
experiment.exposure_time1.0
experiment.number_of_frames10
experiment.wavelength0.09
experiment.sample_detector_distance2.87
experiment.concentration_min1.1
experiment.concentration_max5.5
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.079
experiment.s_max4.71
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].softwareDAMMIN
fits[0].models[0].pdb_link[]
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fits[0].models[0].type_of_modeldummy
fits[0].models[0].software_version
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fits[0].models[0].model_mw48.915
fits[0].models[0].bead_radius2.75
fits[0].models[0].lognull
fits[0].models[0].symmetry
fits[0].models[0].comment
fits[0].models[0].user104
fits[0].fit_unit1/A
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fits[0].softwarenull
fits[0].chi_square_value0.7
fits[0].p_value0.0
fits[0].fit_residual_plotSASDBG3_fit1_fitresiduals_img.png
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fits[0].fit_lognull
fits[0].software_versionnull
fits[0].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionnull
i0_calibration_standardnull
descriptionnull
experiment_descriptionX-ray synchrotron radiation scattering data from solutions of Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct) in 20 mM Tris 150 mM NaCl, 3% glycerol were collected on the ID14-3 beam line at the ESRF storage ring (Grenoble, France) using a 2D Photon counting Pilatus 1M pixel detector (s = 4π sin θ/λ, where 2θ is the scattering angle). Different solute concentrations in the range 1.10-5.50 mg/ml were measured. 10 successive 1 second frames were collected at a sample temperature of 20 degrees centigrade. SAXS data from the samples and corresponding matched solvent blank were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted. The low angle data collected were obtained from a merged concentration scattering curve.
tags[]
intensity_unitnull
experimental_mw50.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw40.0
porod_mw_errornull
pddf_i059.3
pddf_i0_errornull
guinier_i059.2
guinier_i0_errornull
pddf_rg3.34
pddf_rg_errornull
guinier_rg3.31
guinier_rg_errornull
pddf_dmax13.1
pddf_dmax_errornull
porod_volumenull
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_firstnull
guinier_point_lastnull
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDBG3_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDBG3
statussuccess
started_at2026-08-11T13:59:38.378061+00:00
finished_at2026-08-11T13:59:47.069983+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDBG3",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/nm",
  "project": {
    "title": "Crystal Structure of an Engineered LRRTM2 Synaptic Adhesion Molecule and a Model for Neurexin Binding.",
    "publication": {
      "title": "Crystal Structure of an Engineered LRRTM2 Synaptic Adhesion Molecule and a Model for Neurexin Binding.",
      "author_list": "Paatero A, Rosti K, Shkumatov AV, Sele C, Brunello C, Kysenius K, Singha P, Jokinen V, Huttunen H, Kajander T",
      "journal": "Biochemistry",
      "doi": "10.1021/acs.biochem.5b00971",
      "pmid": "26785044",
      "published_date": "2016 Feb 16"
    },
    "status": "released",
    "submitted_date": "2016-01-25",
    "released_date": "2016-01-26"
  },
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        "type": "Dectris",
        "name": "Pilatus 1M",
        "resolution": 172.0
      },
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      "country": "France",
      "beamline_name": "ID14-3",
      "beam_geometry": "",
      "type_of_source": "X-ray synchrotron",
      "point_source": true,
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    "sample": {
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        {
          "long_name": "Mouse Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct)",
          "short_name": "cLRRTM2 30-380",
          "sequence": "GPMACPPKCRCEKLLFYCDSQGFHSVPNGLPSQLLGLSLRHNQLQSLPNGVFDKLTQLTWLHLDHNQLQSLPNGVFDKLTKLTELILSSNQLQSLPNGTFDKLTNLQNLDLSFNQLQSLPNGVFDKLTNLQTLHLRSNQLQSLPNGVFDKLTSLTFLDLSTNQLQSLPNGVFDKLTNLRELHLEHNQL QSLPNGVFDKLTSLTTLFLQWNQLQSLPNGVFDKLTNLEKLDLTGNQLQSLPNGVFDKLTNLKILLLDNNQLQSLPNGVFDKLKSLTTVGLSGNLWECSPRVCALASWLGSFQGRWEHSILCHSPDHTQGEDILDAVHGFQLCWNLSTTVTAMATTYRDPTTEKLVEKY\r\n",
          "organism": "Mus musculus",
          "uniprot_code": "Q8BGA3",
          "uniprot_range_first": 30,
          "uniprot_range_last": 380,
          "oligomerization": "monomer",
          "molecular_type": "protein",
          "uniprot_sequence": "MGLHFKWPLGAPMLAAIYAMSVVLKMLPALGMACPPKCRCEKLLFYCDSQGFHSVPNATD\nKGSLGLSLRHNHITALERDQFASFSQLTWLHLDHNQISTVKEDAFQGLYKLKELILSSNK\nIFYLPNTTFTQLINLQNLDLSFNQLSSLHPELFYGLRKLQTLHLRSNSLRTIPVRLFWDC\nRSLEFLDLSTNRLRSLARNGFAGLIKLRELHLEHNQLTKINFAHFLRLSSLHTLFLQWNK\nISNLTCGMDWTWSTLEKLDLTGNEIKAIDLTVFETMPNLKILLMDNNKLNSLDSKILNSL\nKSLTTVGLSGNLWECSPRVCALASWLGSFQGRWEHSILCHSPDHTQGEDILDAVHGFQLC\nWNLSTTVTAMATTYRDPTTEYTKISSSSYHVGDKEIPTTAGIAVTTEEHFPEPDNAIFTQ\nRVITGTMALLFSFFFIIFIVFISRKCCPPTLRRIRQCSMIQNHRQLRSQTRLHMSNMSDQ\nGPYNEYEPTHEGPFIIINGYGQCKCQQLPYKECEV",
          "mw": 40.01,
          "total_mw": 40.01,
          "number_molecules": 1,
          "complex_state": false,
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View the complete manifest.json source
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