SASDC48

ScsC-ScsBalpha complex

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Single concentration 最后更新:2020-06-15T11:36:42.269791+02:00
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1. 样品、组分与实验条件 Sample & Experiment

样品 1 · ScsC-ScsBalpha complex

浓度0.56 – 4.5 缓冲液 / pH10mM HEPES, 150mM NaCl / 7.5
实验温度10.0 设备 / 束线Australian Synchrotron / SAXS/WAXS
波长0.1033 nm曝光1.0 s × 13

分子组分

组分类型 / 物种UniProt 与构建体寡聚状态分子量
DsbA-like protein
查看序列
SNAALNAAQEKEVRALVRDTLVSNPEILEEAIMALQTKKADEQQAQFRQALASEHDALYNDAASPRIGAKDAKLVLVSFTDYNCPYCKRFDPLLEKITEQYPDVAVIIKPLPFKGESSAKASQAVLSVWKEDPKAFLALHQRLMQKKTMLDNASIEDAMKSTNTSKIKLTDDSLKTLQNNLELSRKLGIQGTPATVIGDTILPGAVDYDQLEIIVKEQLAKVKK
proteinProteus mirabilisC2LPE222–243trimer分子数 324.768 kDa
Putative metal resistance protein
查看序列
MHHHHHHSSGVDLGTENLYFQSNADTGWLTMPDNDHAQVRATADKSSTGDVKILLEVQLAPGWKTYWRSPGEGGVAPEINWTQSVSDMIWHWPSPSAFDVAGIHTQGYDKEVVFPIELKSVDSDNLNGVLTLSTCSNVCILTDYSLNLDLNEPAPADFEWQYNQAMAKVPVTSGLISAVSSDYRNSQLTLSLQREQGDWHQPNIYLDPPQGMLYGIPQLTAKGDHLSVTVDVTDDWGDAAGDITGKALSFVVTDDGYSRQVNDTIGQGDSASLPTADS
proteinProteus mirabilisB4EV2022–275monomer分子数 130.343 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
1372[3]0.010537851–0.29986023 1/A含误差列缺失 010sasbdb/entries/48/sasdc48/source/SASDC48.dat
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2. SASBDB 报告的指标 Reported Results

指标方法数值误差单位
dmaxP(r)11.53.0Å
i0Guinier0.040570.000121/cm
i0P(r)0.040260.00011/cm
mwExperimental95.0—kDa
mwGuinier I(0)95.05.0kDa
mwPorod119.0—kDa
porod_volumePorod145.0—ų
rgGuinier3.920.02Å
rgP(r)3.870.01Å

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。

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3. 来源拟合与模型 Source Fits & Models

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4. 来源文件索引 Source Files

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5. 实验说明与论文 Experiment & Publication

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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10mM HEPES, 150mM NaCl缓冲液浓度—
pH7.5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2016-11-02储存 / 测量温度4.0 / 10.0
曝光时间1.0帧数13
波长0.1033样品-探测器距离2.68
光源X-ray synchrotron探测器Pilatus 1M
机构 / 束线Australian Synchrotron / SAXS/WAXS · Melbourne, Australia
q 范围0.105 – 2.999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
curvesasbdb/entries/48/sasdc48/source/SASDC48.datdownloaded19412e576f575a87943c6109645f6c63ff5984fbd5fdeca35fe0766ecd321c83a51b1下载查看原文件源站
full_entry_zipsasbdb/entries/48/sasdc48/source/SASDC48.zipdownloaded3989725c6ad30578b24129f0fdf84662bf714af74a7bc05447b08967709a71037d3378下载查看原文件源站
pddfsasbdb/entries/48/sasdc48/source/SASDC48.outdownloaded321634a8547854c04a364de741ab87b24e5887d70a97915e121ce62bb3d4ac5e21889下载查看原文件源站
sascifsasbdb/entries/48/sasdc48/source/SASDC48.sascifdownloaded734618945bf974e9917a4e027a1dbbb42e528a81ac4dcd51f0b64657571b5b2d446a78下载查看原文件源站
summarysasbdb/entries/48/sasdc48/source/summary.jsondownloaded9636292803372ae36f00be23c5dcfbd4cf8f9f1be1748fa081ad35dd71dfa34ecbe3下载查看原文件源站
curve:来源记录
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full_entry_zip:来源记录与 ZIP 内部目录(6 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
codeSASDC48
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleDisulfide isomerase activity of the dynamic, trimeric <b><i>Proteus mirabilis</i></b> ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB.
project.publication.titleDisulfide isomerase activity of the dynamic, trimeric <b><i>Proteus mirabilis</i></b> ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB.
project.publication.author_listFurlong EJ, Choudhury HG, Kurth F, Duff AP, Whitten AE, Martin JL
project.publication.journalJ Biol Chem
project.publication.doi10.1074/jbc.RA118.001860
project.publication.pmid29491145
project.publication.published_date2018 Apr 20
project.statusreleased
project.submitted_date2017-10-05
project.released_date2018-02-21
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDC48.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDC48.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDC48_dat_img.png
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intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDC48_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDC48.sascif
experiment.instrument.detector.typeDectris
experiment.instrument.detector.namePilatus 1M
experiment.instrument.detector.resolution172.0
experiment.instrument.nameAustralian Synchrotron
experiment.instrument.cityMelbourne
experiment.instrument.countryAustralia
experiment.instrument.beamline_nameSAXS/WAXS
experiment.instrument.beam_geometryPoint
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_nameDsbA-like protein
experiment.sample.molecule[0].short_nameScsC
experiment.sample.molecule[0].sequenceSNAALNAAQEKEVRALVRDTLVSNPEILEEAIMALQTKKADEQQAQFRQALASEHDALYNDAASPRIGAKDAKLVLVSFTDYNCPYCKRFDPLLEKITEQYPDVAVIIKPLPFKGESSAKASQAVLSVWKEDPKAFLALHQRLMQKKTMLDNASIEDAMKSTNTSKIKLTDDSLKTLQNNLELSRKLGIQGTPATVIGDTILPGAVDYDQLEIIVKEQLAKVKK
experiment.sample.molecule[0].organismProteus mirabilis
experiment.sample.molecule[0].uniprot_codeC2LPE2
experiment.sample.molecule[0].uniprot_range_first22
experiment.sample.molecule[0].uniprot_range_last243
experiment.sample.molecule[0].oligomerizationtrimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequencenull
experiment.sample.molecule[0].mw24.768
experiment.sample.molecule[0].total_mw74.304
experiment.sample.molecule[0].number_molecules3
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.molecule[1].long_namePutative metal resistance protein
experiment.sample.molecule[1].short_nameScsB
experiment.sample.molecule[1].sequenceMHHHHHHSSGVDLGTENLYFQSNADTGWLTMPDNDHAQVRATADKSSTGDVKILLEVQLAPGWKTYWRSPGEGGVAPEINWTQSVSDMIWHWPSPSAFDVAGIHTQGYDKEVVFPIELKSVDSDNLNGVLTLSTCSNVCILTDYSLNLDLNEPAPADFEWQYNQAMAKVPVTSGLISAVSSDYRNSQLTLSLQREQGDWHQPNIYLDPPQGMLYGIPQLTAKGDHLSVTVDVTDDWGDAAGDITGKALSFVVTDDGYSRQVNDTIGQGDSASLPTADS
experiment.sample.molecule[1].organismProteus mirabilis
experiment.sample.molecule[1].uniprot_codeB4EV20
experiment.sample.molecule[1].uniprot_range_first22
experiment.sample.molecule[1].uniprot_range_last275
experiment.sample.molecule[1].oligomerizationmonomer
experiment.sample.molecule[1].molecular_typeprotein
experiment.sample.molecule[1].uniprot_sequenceMVRSFLIALMLMLFSLSSLAADTGWLTMPDNDHAQVRATADKSSTGDVKILLEVQLAPGW KTYWRSPGEGGVAPEINWTQSVSDMIWHWPSPSAFDVAGIHTQGYDKEVVFPIELKSVDS DNLNGVLTLSTCSNVCILTDYSLNLDLNEPAPADFEWQYNQAMAKVPVTSGLISAVSSDY RNSQLTLSLQREQGDWHQPNIYLDPPQGMLYGIPQLTAKGDHLSVTVDVTDDWGDAAGDI TGKALSFVVTDDGYSRQVNDTIGQGDSASLPTADSGVGLWSILAFALLGGLILNLMPCVL PVLAMKLGSILHIEKRDTGAIRKQFSVSVVGILVSFWALALFMTVLRYSQEAIGWGIQFQ SPWFIGFMVLITAIFTANLFGLFELRLSSNMNTKIATAGGQGYSRHFWEGAFATLLATPC SAPFLGTAVAYALIAPLSELWLIFTALGLGMSLPWIMVAMFPSIAKVLPKPGKWMNRLRV VLGFMMLLSCIWLITLLIPHFGIGIVAAIFVAIALILLFAIAKHYGKKTLFASMVITLIL GGTSYLFIAQPDTQTLAGQDHVNWQPLSEEAIHQALAENKRVFIDVTADWCVTCKANKYN VLLRDDVQKALSEPDVVALRGDWTKPSEQITQFLKQRGQVAVPFNQIYGPCNKEGEILPP LLNKDLMLTILSEAKGAQ
experiment.sample.molecule[1].mw30.343
experiment.sample.molecule[1].total_mw30.343
experiment.sample.molecule[1].number_molecules1
experiment.sample.molecule[1].complex_stateFalse
experiment.sample.molecule[1].deuterationnull
experiment.sample.molecule[1].molecule_sourcebiological
experiment.sample.molecule[1].molecule_descriptionnull
experiment.sample.buffer.name10mM HEPES, 150mM NaCl
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameScsC-ScsBalpha 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[0].short_nameANSTO
experiment.contributor[0].affiliation[0].addressKirrawee DC, NSW 2232, Australia
experiment.contributor[0].affiliation[0].full_nameAustralian Nuclear Science and Technology Organisation
experiment.contributor[0].affiliation[0].webpage
experiment.contributor[0].contributor_nameAndrew
experiment.contributor[0].contributor_surnameWhitten
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2016-11-02
experiment.storage_temperature4.0
experiment.cell_temperature10.0
experiment.exposure_time1.0
experiment.number_of_frames13
experiment.wavelength0.1033
experiment.sample_detector_distance2.68
experiment.concentration_min0.56
experiment.concentration_max4.5
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.105
experiment.s_max2.999
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[0].models[0].model_plothttps://www.sasbdb.org/media/pdb_file/images/SASDC48_fit1_model1_img.png
fits[0].models[0].softwareSASREF
fits[0].models[0].pdb_link[]
fits[0].models[0].model_titlenull
fits[0].models[0].type_of_modelatomic
fits[0].models[0].software_version7.d
fits[0].models[0].model_datahttps://www.sasbdb.org/media/pdb_file/SASDC48_fit1_model1.pdb
fits[0].models[0].model_mw99.99
fits[0].models[0].bead_radius1.9
fits[0].models[0].loghttps://www.sasbdb.org/media/log_files/run1_ZoMbNC2.log
fits[0].models[0].symmetryP1
fits[0].models[0].commentOverall symmetry is P1, but the ScsC component possesses P3 symmetry
fits[0].models[0].user111
fits[0].fit_unit1/A
fits[0].fit_plothttps://www.sasbdb.org/media/fitting_files/scattering_plots/SASDC48_fit1_fit_img.png
fits[0].softwareSASREF
fits[0].chi_square_value1.7956
fits[0].p_value0.0
fits[0].fit_residual_plotSASDC48_fit1_fitresiduals_img.png
fits[0].fit_datahttps://www.sasbdb.org/media/fitting_files/SASDC48_fit1.fit
fits[0].fit_loghttps://www.sasbdb.org/media/fitting_files/log_files/run1_ZTJcGes.log
fits[0].software_version7.d
fits[0].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version4.6
i0_calibration_standardnull
descriptionnull
experiment_descriptionX-ray synchrotron radiation scattering data from solutions of Suppressor of Copper Sensitivity C protein (ScsC) complexed with the alpha domain of the Suppressor of Copper Sensitivity B protein from Proteus mirabilis in 10 mM HEPES 100mM NaCl, pH 7.5 were collected on the SAXS/WAXS beam line of the Australian Synchrotron (Melbourne, Australia) using a 2D Photon counting Pilatus 1M-W pixel detector (s = 4π sin θ/λ, where 2θ is the scattering angle). Thirteen successive 1 second frames were collected across solute concentrations of 0.56-4.50 mg/ml. The SAXS data displayed this entry was derived from a 0.56 mg/ml sample. The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted. Small-angle neutron scattering data with contrast variation were also collected on the QUOKKA instrument at the Australian Nuclear Science and Technology Organisation at a solute concentration of ~5.0 mg/ml. A rigid-body model was co-refined against the SAXS and SANS data using using SASREF (v 7.d), and this model is shown, together with the X-ray data and correspond fit. Details of the SANS data collection, corresponding fits, and additional analysis are contained in a downloadable zip archive.
tags[]
intensity_unit1/cm
experimental_mw95.0
experimental_mw_errornull
guinier_i0_mw95.0
guinier_i0_mw_error5.0
porod_mw119.0
porod_mw_errornull
pddf_i00.04026
pddf_i0_error0.0001
guinier_i00.04057
guinier_i0_error0.00012
pddf_rg3.87
pddf_rg_error0.01
guinier_rg3.92
guinier_rg_error0.02
pddf_dmax11.5
pddf_dmax_error3.0
porod_volume145.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first1
guinier_point_last30
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDC48_datloglog_img.png
symmetrynull
last_modified2020-06-15T11:36:42.269791+02:00
bragg_peak[]
manifest.json:36 个字段值
字段路径原始值
codeSASDC48
statussuccess
started_at2026-08-11T15:45:23.446957+00:00
finished_at2026-08-11T15:45:32.777217+00:00
source_last_modified2020-06-15T11:36:42.269791+02:00
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查看完整 summary.json 原文
{
  "code": "SASDC48",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Disulfide isomerase activity of the dynamic, trimeric <b><i>Proteus mirabilis</i></b> ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB.",
    "publication": {
      "title": "Disulfide isomerase activity of the dynamic, trimeric <b><i>Proteus mirabilis</i></b> ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB.",
      "author_list": "Furlong EJ, Choudhury HG, Kurth F, Duff AP, Whitten AE, Martin JL",
      "journal": "J Biol Chem",
      "doi": "10.1074/jbc.RA118.001860",
      "pmid": "29491145",
      "published_date": "2018 Apr 20"
    },
    "status": "released",
    "submitted_date": "2017-10-05",
    "released_date": "2018-02-21"
  },
  "pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDC48.out",
  "intensities_data": "https://www.sasbdb.org/media/intensities_files/SASDC48.dat",
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  "intensities_kratky_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDC48_kratky_img.png",
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  "intensities_guinier_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDC48_guinier_img.png",
  "sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDC48.sascif",
  "experiment": {
    "instrument": {
      "detector": {
        "type": "Dectris",
        "name": "Pilatus 1M",
        "resolution": 172.0
      },
      "name": "Australian  Synchrotron",
      "city": "Melbourne",
      "country": "Australia",
      "beamline_name": "SAXS/WAXS",
      "beam_geometry": "Point",
      "type_of_source": "X-ray synchrotron",
      "point_source": true,
      "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": "DsbA-like protein",
          "short_name": "ScsC",
          "sequence": "SNAALNAAQEKEVRALVRDTLVSNPEILEEAIMALQTKKADEQQAQFRQALASEHDALYNDAASPRIGAKDAKLVLVSFTDYNCPYCKRFDPLLEKITEQYPDVAVIIKPLPFKGESSAKASQAVLSVWKEDPKAFLALHQRLMQKKTMLDNASIEDAMKSTNTSKIKLTDDSLKTLQNNLELSRKLGIQGTPATVIGDTILPGAVDYDQLEIIVKEQLAKVKK",
          "organism": "Proteus mirabilis",
          "uniprot_code": "C2LPE2",
          "uniprot_range_first": 22,
          "uniprot_range_last": 243,
          "oligomerization": "trimer",
          "molecular_type": "protein",
          "uniprot_sequence": null,
          "mw": 24.768,
          "total_mw": 74.304,
          "number_molecules": 3,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        },
        {
          "long_name": "Putative metal resistance protein",
          "short_name": "ScsB",
          "sequence": "MHHHHHHSSGVDLGTENLYFQSNADTGWLTMPDNDHAQVRATADKSSTGDVKILLEVQLAPGWKTYWRSPGEGGVAPEINWTQSVSDMIWHWPSPSAFDVAGIHTQGYDKEVVFPIELKSVDSDNLNGVLTLSTCSNVCILTDYSLNLDLNEPAPADFEWQYNQAMAKVPVTSGLISAVSSDYRNSQLTLSLQREQGDWHQPNIYLDPPQGMLYGIPQLTAKGDHLSVTVDVTDDWGDAAGDITGKALSFVVTDDGYSRQVNDTIGQGDSASLPTADS",
          "organism": "Proteus mirabilis",
          "uniprot_code": "B4EV20",
          "uniprot_range_first": 22,
          "uniprot_range_last": 275,
          "oligomerization": "monomer",
          "molecular_type": "protein",
          "uniprot_sequence": "MVRSFLIALMLMLFSLSSLAADTGWLTMPDNDHAQVRATADKSSTGDVKILLEVQLAPGW\nKTYWRSPGEGGVAPEINWTQSVSDMIWHWPSPSAFDVAGIHTQGYDKEVVFPIELKSVDS\nDNLNGVLTLSTCSNVCILTDYSLNLDLNEPAPADFEWQYNQAMAKVPVTSGLISAVSSDY\nRNSQLTLSLQREQGDWHQPNIYLDPPQGMLYGIPQLTAKGDHLSVTVDVTDDWGDAAGDI\nTGKALSFVVTDDGYSRQVNDTIGQGDSASLPTADSGVGLWSILAFALLGGLILNLMPCVL\nPVLAMKLGSILHIEKRDTGAIRKQFSVSVVGILVSFWALALFMTVLRYSQEAIGWGIQFQ\nSPWFIGFMVLITAIFTANLFGLFELRLSSNMNTKIATAGGQGYSRHFWEGAFATLLATPC\nSAPFLGTAVAYALIAPLSELWLIFTALGLGMSLPWIMVAMFPSIAKVLPKPGKWMNRLRV\nVLGFMMLLSCIWLITLLIPHFGIGIVAAIFVAIALILLFAIAKHYGKKTLFASMVITLIL\nGGTSYLFIAQPDTQTLAGQDHVNWQPLSEEAIHQALAENKRVFIDVTADWCVTCKANKYN\nVLLRDDVQKALSEPDVVALRGDWTKPSEQITQFLKQRGQVAVPFNQIYGPCNKEGEILPP\nLLNKDLMLTILSEAKGAQ",
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          "number_molecules": 1,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        }
      ],
      "buffer": {
        "name": "10mM HEPES, 150mM NaCl",
        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 7.5,
        "deuteration": null
      },
      "purity_method": null,
      "name": "ScsC-ScsBalpha complex",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": "ANSTO",
            "address": "Kirrawee DC, NSW 2232, Australia",
            "full_name": "Australian Nuclear Science and Technology Organisation",
            "webpage": ""
          }
        ],
        "contributor_name": "Andrew",
        "contributor_surname": "Whitten",
        "orcid": null
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2016-11-02",
    "storage_temperature": 4.0,
    "cell_temperature": 10.0,
    "exposure_time": 1.0,
    "number_of_frames": 13,
    "wavelength": 0.1033,
    "sample_detector_distance": 2.68,
    "concentration_min": 0.56,
    "concentration_max": 4.5,
    "sample_volume": null,
    "flow_rate": null,
    "s_min": 0.105,
    "s_max": 2.999,
    "total_exposure_time": null,
    "seccolumn": null
  },
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    {
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        {
          "model_plot": "https://www.sasbdb.org/media/pdb_file/images/SASDC48_fit1_model1_img.png",
          "software": "SASREF",
          "pdb_link": [],
          "model_title": null,
          "type_of_model": "atomic",
          "software_version": "7.d",
          "model_data": "https://www.sasbdb.org/media/pdb_file/SASDC48_fit1_model1.pdb",
          "model_mw": 99.99,
          "bead_radius": 1.9,
          "log": "https://www.sasbdb.org/media/log_files/run1_ZoMbNC2.log",
          "symmetry": "P1",
          "comment": "Overall symmetry is P1, but the ScsC component possesses P3 symmetry",
          "user": 111
        }
      ],
      "fit_unit": "1/A",
      "fit_plot": "https://www.sasbdb.org/media/fitting_files/scattering_plots/SASDC48_fit1_fit_img.png",
      "software": "SASREF",
      "chi_square_value": 1.7956,
      "p_value": 0.0,
      "fit_residual_plot": "SASDC48_fit1_fitresiduals_img.png",
      "fit_data": "https://www.sasbdb.org/media/fitting_files/SASDC48_fit1.fit",
      "fit_log": "https://www.sasbdb.org/media/fitting_files/log_files/run1_ZTJcGes.log",
      "software_version": "7.d",
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  "pddf_software": "ATSAS GNOM",
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  "i0_calibration_standard": null,
  "description": null,
  "experiment_description": "X-ray synchrotron radiation scattering data from solutions of Suppressor of Copper Sensitivity C protein (ScsC) complexed with the alpha domain of the Suppressor of Copper Sensitivity B protein from Proteus mirabilis in 10 mM HEPES 100mM NaCl, pH 7.5 were collected on the SAXS/WAXS beam line of the Australian Synchrotron (Melbourne, Australia) using a 2D Photon counting Pilatus 1M-W pixel detector (s = 4π sin θ/λ, where 2θ is the scattering angle). Thirteen successive 1 second frames were collected across solute concentrations of 0.56-4.50 mg/ml. The SAXS data displayed this entry was derived from a 0.56 mg/ml sample. The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted. Small-angle neutron scattering data with contrast variation were also collected on the QUOKKA instrument at the Australian Nuclear Science and Technology Organisation at a solute concentration of ~5.0 mg/ml. A rigid-body model was co-refined against the SAXS and SANS data using using SASREF (v 7.d), and this model is shown, together with the X-ray data and correspond fit. Details of the SANS data collection, corresponding fits, and additional analysis are contained in a downloadable zip archive.",
  "tags": [],
  "intensity_unit": "1/cm",
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  "pddf_dmax_error": 3.0,
  "porod_volume": 145.0,
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  "estimated_volume": null,
  "estimated_volume_error": null,
  "guinier_point_first": 1,
  "guinier_point_last": 30,
  "pddf_point_first": null,
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  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDC48_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2020-06-15T11:36:42.269791+02:00",
  "bragg_peak": []
}
查看完整 manifest.json 原文
{
  "code": "SASDC48",
  "status": "success",
  "started_at": "2026-08-11T15:45:23.446957+00:00",
  "finished_at": "2026-08-11T15:45:32.777217+00:00",
  "source_last_modified": "2020-06-15T11:36:42.269791+02:00",
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