SASDAR6

human CSF-1:CSF-1R extracellular signalling complex

Data type: SASBDB experimental data Status: Published Curve type: Merged Last updated: 2023-05-25T11:21:52.654103+02:00

SAXS data acquisition for the glycosylated ternary hCSF-1:hCSF-1R full ectodomain complex (MW including glycans: 158 kDa) and subsequent data processing were performed as described in Elegheert et al., 2011 and Felix et al., 2013 respectively (see references). Rigid-body refinements of the hCSF-1:hCSF-1R complex were performed using the online version of SASREF. For each run, data to 0.25 angstrom-1 was used while imposing P2 symmetry. The crystal structure of full length hCSF-1:hCSF-1R without D1 was taken as a starting rigid-body core (PDB ID: 4WRM). D1 was added as a separate rigid body with a contact restraint of 4 angstrom between its C-terminus and the N-terminus of hCSF-1RD2-D5, as well as 5 N-linked glycans containing a 'dummy' Asparagine residue (Asn-GlcNac2Man5) with 1 angstrom restraints to the C-alpha of truncated Asparagine residues on hCSF-1RD2-D5 (N73, N153, N240, N275 and N353). The SASREF calculated fit of the model to the experimental data gave a chi-squared of 1.65, recalculation of the fit using Crysol and FoXS gave a chi-squared of 3.0 and 1.5 respectively. Here, the fit calculated with FoXS is presented. Felix, J., Elegheert, J., Gutsche, I., Shkumatov, A.V., Wen, Y., Bracke, N., Pannecoucke, E., Vandenberghe, I., Devreese, B., Svergun, D.I., et al. (2013). Human IL-34 and CSF-1 establish structurally similar extracellular assemblies with their common hematopoietic receptor. Structure 21, 528-539. Elegheert, J., Desfosses, A., Shkumatov, A.V., Wu, X., Bracke, N., Verstraete, K., Van Craenenbroeck, K., Brooks, B.R., Svergun, D.I., Vergauwen, B., et al. (2011). Extracellular Complexes of the Hematopoietic Human and Mouse CSF-1 Receptor Are Driven by Common Assembly Principles. Structure 19, 1762-1772.

▼

1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · human CSF-1:CSF-1R extracellular signalling complex

Concentration0.5 – 10.0 mg/mlBuffer / pH50 mM NaH2PO4, 100 m / 7.4
Experimental temperature10.0 Facility / beamlineDORIS III, DESY / EMBL X33
Wavelength0.15 nmExposure8.0 s × 15

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Macrophage colony-stimulating factor 1
View sequence
EEVSEYCSHMIGSGHLQSLQRLIDSQMETSCQITFEFVDQEQLKDPVCYLKKAFLLVQDIMEDTMRFRDNTPNAIAIVQLQELSLRLKSCFTKDYEEHDKACVRTFYETPLQLLEKVKNVFNETKNLLDKDWNIFSKNCNNSFAECSSQ
proteinHomo sapiens——–—dimerMolecule count 217.436 kDa
Macrophage colony-stimulating factor 1 receptor
View sequence
IPVIEPSVPELVVKPGATVTLRCVGNGSVEWDGPPSPHWTLYSDGSSSILSTNNATFQNTGTYRCTEPGDPLGGSAAIHLYVKDPARPWNVLAQEVVVFEDQDALLPCLLTDPVLEAGVSLVRVRGRPLMRHTNYSFSPWHGFTIHRAKFIQSQDYQCSALMGGRKVMSISIRLKVQKVIPGPPALTLVPAELVRIRGEAAQIVCSASSVDVNFDVFLQHNNTKLAIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASNVQGKHSTSMFFRVVESAYLNLSSEQNLIQEVTVGEGLNLKVMVEAYPGLQGFNWTYLGPFSDHQPEPKLANATTKDTYRHTFTLSLPRLKPSEAGRYSFLARNPGGWRALTFELTLRYPPEVSVIWTFINGSGTLLCAASGYPQPNVTWLQCSGHTDRCDEAQVLQVWDDPYPEVLSQEPFHKVTVQSLLTVETLEHNQTYECRAHNSVGSGSWAFIPISAGTKHHHHHH
proteinHomo sapiens——–—dimerMolecule count 253.554 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11847[3]0.0731–4.84 1/nmHas uncertainty columnMissing 00sasbdb/entries/r6/sasdar6/source/SASDAR6.dat
▼

2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)17.9—nm
i0Guinier188.32——
i0P(r)187.7——
mwExperimental185.0—kDa
mwGuinier I(0)185.0—kDa
porod_volumePorod298.52—nm³
rgGuinier5.67—nm
rgP(r)5.67—nm

These values are reported by SASBDB; SAXSdb did not recalculate them from the experimental curve.

▼

3. Source Fits and Models Source Fits & Models

▶

4. Source File Index Source Files

▶

5. Experiment Description and Publication Experiment & Publication

▼

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 NaH2PO4, 100 mBuffer concentration—
pH7.4Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2009-03-13Storage / measurement temperature10.0 / 10.0
Exposure time8.0Frames15
Wavelength0.15Sample-to-detector distance2.7
SourceX-ray synchrotronDetectorPilatus 1M-W
Facility / beamlineDORIS III, DESY / EMBL X33 · Hamburg, Germany
q range0.073 – 4.84Sample 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

CategoryFileStatusSizeChecksumDownload and View
curvesasbdb/entries/r6/sasdar6/source/SASDAR6.datdownloaded8326891947cfad45cc702d1ea6c32656c0f508e968d1d568905f6d723942cb2cb27e4DownloadView source fileSource site
full_entry_zipsasbdb/entries/r6/sasdar6/source/SASDAR6.zipdownloaded189415fdd0a9f406b90235019be34be7233512f657605c7f32c1c0f99499494e8f0982DownloadView source fileSource site
pddfsasbdb/entries/r6/sasdar6/source/SASDAR6.outdownloaded383267634227e518f56bcd47818421b23dc09e2ae45046860549ad751143b295f4dacDownloadView source fileSource site
sascifsasbdb/entries/r6/sasdar6/source/SASDAR6.sascifdownloaded1161369a9d52576eb791e63db4d02a32e32518f3ad1bceff35401d0f0de8271cdc3d4eeDownloadView source fileSource site
summarysasbdb/entries/r6/sasdar6/source/summary.jsondownloaded10079c46e6cb86738bfbf0a9943f904d4b2711e47bbe6b1d76689049806a921558a8eDownloadView source fileSource site
curve:source record
{
  "path": "/data/saxsdb/sasbdb/entries/r6/sasdar6/source/SASDAR6.dat",
  "role": "curve",
  "sha256": "91947cfad45cc702d1ea6c32656c0f508e968d1d568905f6d723942cb2cb27e4",
  "size": 83268,
  "status": "downloaded",
  "url": "https://www.sasbdb.org/media/intensities_files/SASDAR6.dat"
}
full_entry_zip:source record and ZIP contents (4 items)
{
  "path": "/data/saxsdb/sasbdb/entries/r6/sasdar6/source/SASDAR6.zip",
  "role": "full_entry_zip",
  "sha256": "fdd0a9f406b90235019be34be7233512f657605c7f32c1c0f99499494e8f0982",
  "size": 189415,
  "status": "downloaded",
  "url": "https://www.sasbdb.org/media/zip_directories/SASDAR6.zip",
  "zip_member_count": 4,
  "zip_members": [
    {
      "crc32": "b44f5d4e",
      "name": "SASDAR6/experimental_data/SASDAR6.dat",
      "size": 83268
    },
    {
      "crc32": "69d91eda",
      "name": "SASDAR6/pddf/SASDAR6.out",
      "size": 38326
    },
    {
      "crc32": "9813c69c",
      "name": "SASDAR6/SASDAR6_fit1.dat",
      "size": 40091
    },
    {
      "crc32": "e7e1558b",
      "name": "SASDAR6/SASDAR6_fit1_model1.pdb",
      "size": 679936
    }
  ],
  "zip_validation": "central_directory_readable"
}
pddf:source record
{
  "path": "/data/saxsdb/sasbdb/entries/r6/sasdar6/source/SASDAR6.out",
  "role": "pddf",
  "sha256": "7634227e518f56bcd47818421b23dc09e2ae45046860549ad751143b295f4dac",
  "size": 38326,
  "status": "downloaded",
  "url": "https://www.sasbdb.org/media/p_of_R_files/SASDAR6.out"
}
sascif:source record
{
  "path": "/data/saxsdb/sasbdb/entries/r6/sasdar6/source/SASDAR6.sascif",
  "role": "sascif",
  "sha256": "a9d52576eb791e63db4d02a32e32518f3ad1bceff35401d0f0de8271cdc3d4ee",
  "size": 1161369,
  "status": "downloaded",
  "url": "https://www.sasbdb.org/media/sascif/sascif_files/SASDAR6.sascif"
}
summary:source record
{
  "path": "/data/saxsdb/sasbdb/entries/r6/sasdar6/source/summary.json",
  "sha256": "c46e6cb86738bfbf0a9943f904d4b2711e47bbe6b1d76689049806a921558a8e",
  "size": 10079,
  "status": "downloaded",
  "url": "https://www.sasbdb.org/rest-api/entry/summary/SASDAR6/"
}

All source fields (unfiltered)

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

summary.json:173 field values
Field pathRaw value
codeSASDAR6
statusPublished
type_of_curveMerged
angular_unit1/nm
project.titleStructure and Assembly Mechanism of the Signaling Complex Mediated by Human CSF-1.
project.publication.titleStructure and Assembly Mechanism of the Signaling Complex Mediated by Human CSF-1.
project.publication.author_listFelix J, De Munck S, Verstraete K, Meuris L, Callewaert N, Elegheert J, Savvides SN
project.publication.journalStructure
project.publication.doi10.1016/j.str.2015.06.019
project.publication.pmid26235028
project.publication.published_date2015 Sep 1
project.statusreleased
project.submitted_date2014-10-24
project.released_date2015-09-01
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDAR6.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDAR6.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDAR6_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDAR6_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDAR6_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDAR6_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDAR6.sascif
experiment.instrument.detector.typeCustom-built
experiment.instrument.detector.namePilatus 1M-W
experiment.instrument.detector.resolution0.172
experiment.instrument.nameDORIS III, DESY
experiment.instrument.cityHamburg
experiment.instrument.countryGermany
experiment.instrument.beamline_nameEMBL X33
experiment.instrument.beam_geometry0.60
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_nameMacrophage colony-stimulating factor 1
experiment.sample.molecule[0].short_namehCSF-1
experiment.sample.molecule[0].sequenceEEVSEYCSHMIGSGHLQSLQRLIDSQMETSCQITFEFVDQEQLKDPVCYLKKAFLLVQDIMEDTMRFRDNTPNAIAIVQLQELSLRLKSCFTKDYEEHDKACVRTFYETPLQLLEKVKNVFNETKNLLDKDWNIFSKNCNNSFAECSSQ
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codenull
experiment.sample.molecule[0].uniprot_range_firstnull
experiment.sample.molecule[0].uniprot_range_lastnull
experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequencenull
experiment.sample.molecule[0].mw17.436
experiment.sample.molecule[0].total_mw34.872
experiment.sample.molecule[0].number_molecules2
experiment.sample.molecule[0].complex_statenull
experiment.sample.molecule[0].deuterationnull
experiment.sample.molecule[0].molecule_sourcebiological
experiment.sample.molecule[0].molecule_descriptionnull
experiment.sample.molecule[1].long_nameMacrophage colony-stimulating factor 1 receptor
experiment.sample.molecule[1].short_namehCSF-1R
experiment.sample.molecule[1].sequenceIPVIEPSVPELVVKPGATVTLRCVGNGSVEWDGPPSPHWTLYSDGSSSILSTNNATFQNTGTYRCTEPGDPLGGSAAIHLYVKDPARPWNVLAQEVVVFEDQDALLPCLLTDPVLEAGVSLVRVRGRPLMRHTNYSFSPWHGFTIHRAKFIQSQDYQCSALMGGRKVMSISIRLKVQKVIPGPPALTLVPAELVRIRGEAAQIVCSASSVDVNFDVFLQHNNTKLAIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASNVQGKHSTSMFFRVVESAYLNLSSEQNLIQEVTVGEGLNLKVMVEAYPGLQGFNWTYLGPFSDHQPEPKLANATTKDTYRHTFTLSLPRLKPSEAGRYSFLARNPGGWRALTFELTLRYPPEVSVIWTFINGSGTLLCAASGYPQPNVTWLQCSGHTDRCDEAQVLQVWDDPYPEVLSQEPFHKVTVQSLLTVETLEHNQTYECRAHNSVGSGSWAFIPISAGTKHHHHHH
experiment.sample.molecule[1].organismHomo sapiens
experiment.sample.molecule[1].uniprot_codenull
experiment.sample.molecule[1].uniprot_range_firstnull
experiment.sample.molecule[1].uniprot_range_lastnull
experiment.sample.molecule[1].oligomerizationdimer
experiment.sample.molecule[1].molecular_typeprotein
experiment.sample.molecule[1].uniprot_sequencenull
experiment.sample.molecule[1].mw53.554
experiment.sample.molecule[1].total_mw107.108
experiment.sample.molecule[1].number_molecules2
experiment.sample.molecule[1].complex_statenull
experiment.sample.molecule[1].deuterationnull
experiment.sample.molecule[1].molecule_sourcebiological
experiment.sample.molecule[1].molecule_descriptionnull
experiment.sample.buffer.name50 mM NaH2PO4, 100 m
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.4
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.namehuman CSF-1:CSF-1R extracellular signalling complex
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[]
experiment.contributor[0].contributor_nameJan
experiment.contributor[0].contributor_surnameFelix
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitmg/ml
experiment.date2009-03-13
experiment.storage_temperature10.0
experiment.cell_temperature10.0
experiment.exposure_time8.0
experiment.number_of_frames15
experiment.wavelength0.15
experiment.sample_detector_distance2.7
experiment.concentration_min0.5
experiment.concentration_max10.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.073
experiment.s_max4.84
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[0].models[0].model_plothttps://www.sasbdb.org/media/pdb_file/images/SASDAR6_fit1_model1_img.png
fits[0].models[0].softwareSASREF
fits[0].models[0].pdb_link[0].pdb_code4wrm
fits[0].models[0].pdb_link[0].ext_code4WRM
fits[0].models[0].pdb_link[0].ext_typepdb
fits[0].models[0].pdb_link[0].difference_with_modelnull
fits[0].models[0].model_titlenull
fits[0].models[0].type_of_modelmix
fits[0].models[0].software_version
fits[0].models[0].model_datahttps://www.sasbdb.org/media/pdb_file/SASDAR6_fit1_model1.pdb
fits[0].models[0].model_mw185.2
fits[0].models[0].bead_radius0.0
fits[0].models[0].lognull
fits[0].models[0].symmetryP2
fits[0].models[0].comment
fits[0].models[0].user29
fits[0].fit_unit1/A
fits[0].fit_plothttps://www.sasbdb.org/media/fitting_files/scattering_plots/SASDAR6_fit1_fitfoxs_img.png
fits[0].softwarenull
fits[0].chi_square_value2.236031
fits[0].p_value0.0
fits[0].fit_residual_plotSASDAR6_fit1_fitfoxsresiduals_img.png
fits[0].fit_datahttps://www.sasbdb.org/media/fitting_files/SASDAR6_fit1.dat
fits[0].fit_lognull
fits[0].software_versionnull
fits[0].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionnull
i0_calibration_standardnull
descriptionSAXS data acquisition for the glycosylated ternary hCSF-1:hCSF-1R full ectodomain complex (MW including glycans: 158 kDa) and subsequent data processing were performed as described in Elegheert et al., 2011 and Felix et al., 2013 respectively (see references). Rigid-body refinements of the hCSF-1:hCSF-1R complex were performed using the online version of SASREF. For each run, data to 0.25 angstrom-1 was used while imposing P2 symmetry. The crystal structure of full length hCSF-1:hCSF-1R without D1 was taken as a starting rigid-body core (PDB ID: 4WRM). D1 was added as a separate rigid body with a contact restraint of 4 angstrom between its C-terminus and the N-terminus of hCSF-1RD2-D5, as well as 5 N-linked glycans containing a 'dummy' Asparagine residue (Asn-GlcNac2Man5) with 1 angstrom restraints to the C-alpha of truncated Asparagine residues on hCSF-1RD2-D5 (N73, N153, N240, N275 and N353). The SASREF calculated fit of the model to the experimental data gave a chi-squared of 1.65, recalculation of the fit using Crysol and FoXS gave a chi-squared of 3.0 and 1.5 respectively. Here, the fit calculated with FoXS is presented. Felix, J., Elegheert, J., Gutsche, I., Shkumatov, A.V., Wen, Y., Bracke, N., Pannecoucke, E., Vandenberghe, I., Devreese, B., Svergun, D.I., et al. (2013). Human IL-34 and CSF-1 establish structurally similar extracellular assemblies with their common hematopoietic receptor. Structure 21, 528-539. Elegheert, J., Desfosses, A., Shkumatov, A.V., Wu, X., Bracke, N., Verstraete, K., Van Craenenbroeck, K., Brooks, B.R., Svergun, D.I., Vergauwen, B., et al. (2011). Extracellular Complexes of the Hematopoietic Human and Mouse CSF-1 Receptor Are Driven by Common Assembly Principles. Structure 19, 1762-1772.
experiment_descriptionX-ray synchrotron radiation scattering data from solutions of Macrophage colony-stimulating factor 1 in complex with Macrophage colony-stimulating factor 1 receptor in 50 mM NaH2PO4, 100 mM NaCl (pH 7.4), were collected on the X33 camera on the storage ring DORIS (Hamburg, Germany). Using a 2D Photon counting Pilatus 1M-W pixel detector (s = 4π sin θ/λ, where 2θ is the scattering angle). Different solute concentrations in the range 0.50-10.00 mg/ml were measured. 15 successive 8 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 and the different curves were scaled for protein concentration. The low angle data collected were merged with the highest concentration high angle data to yield the final composite scattering curve.
tags[0]X33
intensity_unitnull
experimental_mw185.0
experimental_mw_errornull
guinier_i0_mw185.0
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i0187.7
pddf_i0_errornull
guinier_i0188.32
guinier_i0_errornull
pddf_rg5.67
pddf_rg_errornull
guinier_rg5.67
guinier_rg_errornull
pddf_dmax17.9
pddf_dmax_errornull
porod_volume298.52
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_plotSASDAR6_datloglog_img.png
symmetrynull
last_modified2023-05-25T11:21:52.654103+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDAR6
statussuccess
started_at2026-08-11T15:14:19.000682+00:00
finished_at2026-08-11T15:14:28.372487+00:00
source_last_modified2023-05-25T11:21:52.654103+02:00
files[0].statusdownloaded
files[0].urlhttps://www.sasbdb.org/rest-api/entry/summary/SASDAR6/
files[0].path/data/saxsdb/sasbdb/entries/r6/sasdar6/source/summary.json
files[0].size10079
files[0].sha256c46e6cb86738bfbf0a9943f904d4b2711e47bbe6b1d76689049806a921558a8e
files[1].statusdownloaded
files[1].urlhttps://www.sasbdb.org/media/intensities_files/SASDAR6.dat
files[1].path/data/saxsdb/sasbdb/entries/r6/sasdar6/source/SASDAR6.dat
files[1].size83268
files[1].sha25691947cfad45cc702d1ea6c32656c0f508e968d1d568905f6d723942cb2cb27e4
files[1].rolecurve
files[2].statusdownloaded
files[2].urlhttps://www.sasbdb.org/media/p_of_R_files/SASDAR6.out
files[2].path/data/saxsdb/sasbdb/entries/r6/sasdar6/source/SASDAR6.out
files[2].size38326
files[2].sha2567634227e518f56bcd47818421b23dc09e2ae45046860549ad751143b295f4dac
files[2].rolepddf
files[3].statusdownloaded
files[3].urlhttps://www.sasbdb.org/media/sascif/sascif_files/SASDAR6.sascif
files[3].path/data/saxsdb/sasbdb/entries/r6/sasdar6/source/SASDAR6.sascif
files[3].size1161369
files[3].sha256a9d52576eb791e63db4d02a32e32518f3ad1bceff35401d0f0de8271cdc3d4ee
files[3].rolesascif
files[4].statusdownloaded
files[4].urlhttps://www.sasbdb.org/media/zip_directories/SASDAR6.zip
files[4].path/data/saxsdb/sasbdb/entries/r6/sasdar6/source/SASDAR6.zip
files[4].size189415
files[4].sha256fdd0a9f406b90235019be34be7233512f657605c7f32c1c0f99499494e8f0982
files[4].rolefull_entry_zip
files[4].zip_member_count4
files[4].zip_validationcentral_directory_readable
View the complete summary.json source
{
  "code": "SASDAR6",
  "status": "Published",
  "type_of_curve": "Merged",
  "angular_unit": "1/nm",
  "project": {
    "title": "Structure and Assembly Mechanism of the Signaling Complex Mediated by Human CSF-1.",
    "publication": {
      "title": "Structure and Assembly Mechanism of the Signaling Complex Mediated by Human CSF-1.",
      "author_list": "Felix J, De Munck S, Verstraete K, Meuris L, Callewaert N, Elegheert J, Savvides SN",
      "journal": "Structure",
      "doi": "10.1016/j.str.2015.06.019",
      "pmid": "26235028",
      "published_date": "2015 Sep 1"
    },
    "status": "released",
    "submitted_date": "2014-10-24",
    "released_date": "2015-09-01"
  },
  "pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDAR6.out",
  "intensities_data": "https://www.sasbdb.org/media/intensities_files/SASDAR6.dat",
  "intensities_log_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDAR6_dat_img.png",
  "intensities_kratky_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDAR6_kratky_img.png",
  "pddf_plot": "https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDAR6_pofr_img.png",
  "intensities_guinier_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDAR6_guinier_img.png",
  "sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDAR6.sascif",
  "experiment": {
    "instrument": {
      "detector": {
        "type": "Custom-built",
        "name": "Pilatus 1M-W",
        "resolution": 0.172
      },
      "name": "DORIS III, DESY",
      "city": "Hamburg",
      "country": "Germany",
      "beamline_name": "EMBL X33",
      "beam_geometry": "0.60",
      "type_of_source": "X-ray synchrotron",
      "point_source": null,
      "line_collimation": null,
      "sample_path_length": null,
      "line_collimation_slitlength": null,
      "line_collimation_integrationwidth": null,
      "xray_energy": null,
      "beam_profile_ah": null,
      "beam_profile_al": null
    },
    "sample": {
      "molecule": [
        {
          "long_name": "Macrophage colony-stimulating factor 1",
          "short_name": "hCSF-1",
          "sequence": "EEVSEYCSHMIGSGHLQSLQRLIDSQMETSCQITFEFVDQEQLKDPVCYLKKAFLLVQDIMEDTMRFRDNTPNAIAIVQLQELSLRLKSCFTKDYEEHDKACVRTFYETPLQLLEKVKNVFNETKNLLDKDWNIFSKNCNNSFAECSSQ\r\n",
          "organism": "Homo sapiens",
          "uniprot_code": null,
          "uniprot_range_first": null,
          "uniprot_range_last": null,
          "oligomerization": "dimer",
          "molecular_type": "protein",
          "uniprot_sequence": null,
          "mw": 17.436,
          "total_mw": 34.872,
          "number_molecules": 2,
          "complex_state": null,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        },
        {
          "long_name": "Macrophage colony-stimulating factor 1 receptor",
          "short_name": "hCSF-1R",
          "sequence": "IPVIEPSVPELVVKPGATVTLRCVGNGSVEWDGPPSPHWTLYSDGSSSILSTNNATFQNTGTYRCTEPGDPLGGSAAIHLYVKDPARPWNVLAQEVVVFEDQDALLPCLLTDPVLEAGVSLVRVRGRPLMRHTNYSFSPWHGFTIHRAKFIQSQDYQCSALMGGRKVMSISIRLKVQKVIPGPPALTLVPAELVRIRGEAAQIVCSASSVDVNFDVFLQHNNTKLAIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASNVQGKHSTSMFFRVVESAYLNLSSEQNLIQEVTVGEGLNLKVMVEAYPGLQGFNWTYLGPFSDHQPEPKLANATTKDTYRHTFTLSLPRLKPSEAGRYSFLARNPGGWRALTFELTLRYPPEVSVIWTFINGSGTLLCAASGYPQPNVTWLQCSGHTDRCDEAQVLQVWDDPYPEVLSQEPFHKVTVQSLLTVETLEHNQTYECRAHNSVGSGSWAFIPISAGTKHHHHHH\r\n\r\n",
          "organism": "Homo sapiens",
          "uniprot_code": null,
          "uniprot_range_first": null,
          "uniprot_range_last": null,
          "oligomerization": "dimer",
          "molecular_type": "protein",
          "uniprot_sequence": null,
          "mw": 53.554,
          "total_mw": 107.108,
          "number_molecules": 2,
          "complex_state": null,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        }
      ],
      "buffer": {
        "name": "50 mM NaH2PO4, 100 m",
        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 7.4,
        "deuteration": null
      },
      "purity_method": null,
      "name": "human CSF-1:CSF-1R extracellular signalling complex",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [],
        "contributor_name": "Jan",
        "contributor_surname": "Felix",
        "orcid": null
      }
    ],
    "concentration_method": null,
    "concentration_unit": "mg/ml",
    "date": "2009-03-13",
    "storage_temperature": 10.0,
    "cell_temperature": 10.0,
    "exposure_time": 8.0,
    "number_of_frames": 15,
    "wavelength": 0.15,
    "sample_detector_distance": 2.7,
    "concentration_min": 0.5,
    "concentration_max": 10.0,
    "sample_volume": null,
    "flow_rate": null,
    "s_min": 0.073,
    "s_max": 4.84,
    "total_exposure_time": null,
    "seccolumn": null
  },
  "fits": [
    {
      "models": [
        {
          "model_plot": "https://www.sasbdb.org/media/pdb_file/images/SASDAR6_fit1_model1_img.png",
          "software": "SASREF",
          "pdb_link": [
            {
              "pdb_code": "4wrm",
              "ext_code": "4WRM",
              "ext_type": "pdb",
              "difference_with_model": null
            }
          ],
          "model_title": null,
          "type_of_model": "mix",
          "software_version": "",
          "model_data": "https://www.sasbdb.org/media/pdb_file/SASDAR6_fit1_model1.pdb",
          "model_mw": 185.2,
          "bead_radius": 0.0,
          "log": null,
          "symmetry": "P2",
          "comment": "",
          "user": 29
        }
      ],
      "fit_unit": "1/A",
      "fit_plot": "https://www.sasbdb.org/media/fitting_files/scattering_plots/SASDAR6_fit1_fitfoxs_img.png",
      "software": null,
      "chi_square_value": 2.236031,
      "p_value": 0.0,
      "fit_residual_plot": "SASDAR6_fit1_fitfoxsresiduals_img.png",
      "fit_data": "https://www.sasbdb.org/media/fitting_files/SASDAR6_fit1.dat",
      "fit_log": null,
      "software_version": null,
      "description": null
    }
  ],
  "estimated_volume_method": null,
  "pddf_software": "ATSAS GNOM",
  "pddf_software_version": null,
  "i0_calibration_standard": null,
  "description": "SAXS data acquisition for the glycosylated ternary hCSF-1:hCSF-1R full ectodomain complex (MW including glycans: 158 kDa) and subsequent data processing were performed as described in Elegheert et al., 2011 and Felix et al., 2013 respectively (see references). Rigid-body refinements of the hCSF-1:hCSF-1R complex were performed using the online version of SASREF. For each run, data to 0.25 angstrom-1 was used while imposing P2 symmetry. The crystal structure of full length hCSF-1:hCSF-1R without D1 was taken as a starting rigid-body core (PDB ID: 4WRM). D1 was added as a separate rigid body with a contact restraint of 4 angstrom between its C-terminus and the N-terminus of hCSF-1RD2-D5, as well as 5 N-linked glycans containing a 'dummy' Asparagine residue (Asn-GlcNac2Man5) with 1 angstrom restraints to the C-alpha of truncated Asparagine residues on hCSF-1RD2-D5 (N73, N153, N240, N275 and N353). The SASREF calculated fit of the model to the experimental data gave a chi-squared of 1.65, recalculation of the fit using Crysol and FoXS gave a chi-squared of 3.0 and 1.5 respectively. Here, the fit calculated with FoXS is presented. Felix, J., Elegheert, J., Gutsche, I., Shkumatov, A.V., Wen, Y., Bracke, N., Pannecoucke, E., Vandenberghe, I., Devreese, B., Svergun, D.I., et al. (2013). Human IL-34 and CSF-1 establish structurally similar extracellular assemblies with their common hematopoietic receptor. Structure 21, 528-539. Elegheert, J., Desfosses, A., Shkumatov, A.V., Wu, X., Bracke, N., Verstraete, K., Van Craenenbroeck, K., Brooks, B.R., Svergun, D.I., Vergauwen, B., et al. (2011). Extracellular Complexes of the Hematopoietic Human and Mouse CSF-1 Receptor Are Driven by Common Assembly Principles. Structure 19, 1762-1772.",
  "experiment_description": "X-ray synchrotron radiation scattering data from solutions of Macrophage colony-stimulating factor 1 in complex with Macrophage colony-stimulating factor 1 receptor in 50 mM NaH2PO4, 100 mM NaCl (pH 7.4), were collected on the X33 camera on the storage ring DORIS (Hamburg, Germany). Using a 2D Photon counting Pilatus 1M-W pixel detector (s = 4π sin θ/λ, where 2θ is the scattering angle). Different solute concentrations in the range 0.50-10.00 mg/ml were measured. 15 successive 8 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 and the different curves were scaled for protein concentration. The low angle data collected were merged with the highest concentration high angle data to yield the final composite scattering curve.",
  "tags": [
    "X33"
  ],
  "intensity_unit": null,
  "experimental_mw": 185.0,
  "experimental_mw_error": null,
  "guinier_i0_mw": 185.0,
  "guinier_i0_mw_error": null,
  "porod_mw": null,
  "porod_mw_error": null,
  "pddf_i0": 187.7,
  "pddf_i0_error": null,
  "guinier_i0": 188.32,
  "guinier_i0_error": null,
  "pddf_rg": 5.67,
  "pddf_rg_error": null,
  "guinier_rg": 5.67,
  "guinier_rg_error": null,
  "pddf_dmax": 17.9,
  "pddf_dmax_error": null,
  "porod_volume": 298.52,
  "porod_volume_error": null,
  "estimated_volume": null,
  "estimated_volume_error": null,
  "guinier_point_first": null,
  "guinier_point_last": null,
  "pddf_point_first": null,
  "pddf_point_last": null,
  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDAR6_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2023-05-25T11:21:52.654103+02:00",
  "bragg_peak": []
}
View the complete manifest.json source
{
  "code": "SASDAR6",
  "status": "success",
  "started_at": "2026-08-11T15:14:19.000682+00:00",
  "finished_at": "2026-08-11T15:14:28.372487+00:00",
  "source_last_modified": "2023-05-25T11:21:52.654103+02:00",
  "files": [
    {
      "status": "downloaded",
      "url": "https://www.sasbdb.org/rest-api/entry/summary/SASDAR6/",
      "path": "/data/saxsdb/sasbdb/entries/r6/sasdar6/source/summary.json",
      "size": 10079,
      "sha256": "c46e6cb86738bfbf0a9943f904d4b2711e47bbe6b1d76689049806a921558a8e"
    },
    {
      "status": "downloaded",
      "url": "https://www.sasbdb.org/media/intensities_files/SASDAR6.dat",
      "path": "/data/saxsdb/sasbdb/entries/r6/sasdar6/source/SASDAR6.dat",
      "size": 83268,
      "sha256": "91947cfad45cc702d1ea6c32656c0f508e968d1d568905f6d723942cb2cb27e4",
      "role": "curve"
    },
    {
      "status": "downloaded",
      "url": "https://www.sasbdb.org/media/p_of_R_files/SASDAR6.out",
      "path": "/data/saxsdb/sasbdb/entries/r6/sasdar6/source/SASDAR6.out",
      "size": 38326,
      "sha256": "7634227e518f56bcd47818421b23dc09e2ae45046860549ad751143b295f4dac",
      "role": "pddf"
    },
    {
      "status": "downloaded",
      "url": "https://www.sasbdb.org/media/sascif/sascif_files/SASDAR6.sascif",
      "path": "/data/saxsdb/sasbdb/entries/r6/sasdar6/source/SASDAR6.sascif",
      "size": 1161369,
      "sha256": "a9d52576eb791e63db4d02a32e32518f3ad1bceff35401d0f0de8271cdc3d4ee",
      "role": "sascif"
    },
    {
      "status": "downloaded",
      "url": "https://www.sasbdb.org/media/zip_directories/SASDAR6.zip",
      "path": "/data/saxsdb/sasbdb/entries/r6/sasdar6/source/SASDAR6.zip",
      "size": 189415,
      "sha256": "fdd0a9f406b90235019be34be7233512f657605c7f32c1c0f99499494e8f0982",
      "role": "full_entry_zip",
      "zip_member_count": 4,
      "zip_validation": "central_directory_readable"
    }
  ]
}