SASDAR6

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

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Merged 最后更新: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. 样品、组分与实验条件 Sample & Experiment

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

浓度0.5 – 10.0 mg/ml缓冲液 / pH50 mM NaH2PO4, 100 m / 7.4
实验温度10.0 设备 / 束线DORIS III, DESY / EMBL X33
波长0.15 nm曝光8.0 s × 15

分子组分

组分类型 / 物种UniProt 与构建体寡聚状态分子量
Macrophage colony-stimulating factor 1
查看序列
EEVSEYCSHMIGSGHLQSLQRLIDSQMETSCQITFEFVDQEQLKDPVCYLKKAFLLVQDIMEDTMRFRDNTPNAIAIVQLQELSLRLKSCFTKDYEEHDKACVRTFYETPLQLLEKVKNVFNETKNLLDKDWNIFSKNCNNSFAECSSQ
proteinHomo sapiens—–—dimer分子数 217.436 kDa
Macrophage colony-stimulating factor 1 receptor
查看序列
IPVIEPSVPELVVKPGATVTLRCVGNGSVEWDGPPSPHWTLYSDGSSSILSTNNATFQNTGTYRCTEPGDPLGGSAAIHLYVKDPARPWNVLAQEVVVFEDQDALLPCLLTDPVLEAGVSLVRVRGRPLMRHTNYSFSPWHGFTIHRAKFIQSQDYQCSALMGGRKVMSISIRLKVQKVIPGPPALTLVPAELVRIRGEAAQIVCSASSVDVNFDVFLQHNNTKLAIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASNVQGKHSTSMFFRVVESAYLNLSSEQNLIQEVTVGEGLNLKVMVEAYPGLQGFNWTYLGPFSDHQPEPKLANATTKDTYRHTFTLSLPRLKPSEAGRYSFLARNPGGWRALTFELTLRYPPEVSVIWTFINGSGTLLCAASGYPQPNVTWLQCSGHTDRCDEAQVLQVWDDPYPEVLSQEPFHKVTVQSLLTVETLEHNQTYECRAHNSVGSGSWAFIPISAGTKHHHHHH
proteinHomo sapiens—–—dimer分子数 253.554 kDa

实验曲线

曲线点数 / 列q 范围误差质量负强度点来源文件
11847[3]0.0731–4.84 1/nm含误差列缺失 00sasbdb/entries/r6/sasdar6/source/SASDAR6.dat

2. SASBDB 报告的指标 Reported Results

指标方法数值误差单位
dmaxP(r)17.9nm
i0Guinier188.32
i0P(r)187.7
mwExperimental185.0kDa
mwGuinier I(0)185.0kDa
porod_volumePorod298.52nm³
rgGuinier5.67nm
rgP(r)5.67nm

这些数值是 SASBDB 来源记录,不是 SAXSdb 对实验曲线重新计算的结果。

3. 来源拟合与模型 Source Fits & Models

4. 来源文件索引 Source Files

5. 实验说明与论文 Experiment & Publication

6. 完整来源记录 Complete Source Record

下列内容直接来自 SASBDB 条目。字段没有值时显示“—”;未声明的单位不会由 SAXSdb 猜测。

打开 SASBDB 原始条目

缓冲液与样品属性

缓冲液名称50 mM NaH2PO4, 100 m缓冲液浓度
pH7.4添加剂
缓冲液说明
纯度测定方法消光系数
吸收值散射对比度
比体积 / 干体积— / —混合物 / 氘代— / —

采集条件与仪器

测量日期2009-03-13储存 / 测量温度10.0 / 10.0
曝光时间8.0帧数15
波长0.15样品-探测器距离2.7
光源X-ray synchrotron探测器Pilatus 1M-W
机构 / 束线DORIS III, DESY / EMBL X33 · Hamburg, Germany
q 范围0.073 – 4.84样品体积 / 流速— / —

SASBDB 原始图

实验 I(q)
实验 I(q)
实验 I(q) log-log
实验 I(q) log-log
Guinier 图
Guinier 图
Kratky 图
Kratky 图
P(r) 图
P(r) 图

可下载文件

类别文件状态大小校验值下载与查看
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full_entry_zipsasbdb/entries/r6/sasdar6/source/SASDAR6.zipdownloaded189415fdd0a9f406b90235019be34be7233512f657605c7f32c1c0f99499494e8f0982下载查看原文件源站
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curve:来源记录
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full_entry_zip:来源记录与 ZIP 内部目录(4 项)
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pddf:来源记录
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sascif:来源记录
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summary:来源记录
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全部来源字段(无筛选)

这里自动展开来源记录中的每一个字段,包括空值、列表成员和页面上方已展示过的字段。

summary.json:173 个字段值
字段路径原始值
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
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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
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fits[0].models[0].pdb_link[0].pdb_code4wrm
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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
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fits[0].softwarenull
fits[0].chi_square_value2.236031
fits[0].p_value0.0
fits[0].fit_residual_plotSASDAR6_fit1_fitfoxsresiduals_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
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 个字段值
字段路径原始值
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
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查看完整 summary.json 原文
{
  "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"
  },
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  "experiment": {
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      "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": {
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          "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
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      "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,
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    "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
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          "software": "SASREF",
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              "difference_with_model": null
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          "bead_radius": 0.0,
          "log": null,
          "symmetry": "P2",
          "comment": "",
          "user": 29
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      "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",
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  "estimated_volume_method": null,
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  "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.",
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  "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": []
}
查看完整 manifest.json 原文
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  "started_at": "2026-08-11T15:14:19.000682+00:00",
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