SASDV39

Human CDAN1-interacting nuclease 1 (frames 692 - 701)

数据类型:SASBDB 实验数据 状态:Published 曲线类型:SEC-SAS 最后更新:2026-02-02T14:39:25.988588+01:00
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1. 样品、组分与实验条件 Sample & Experiment

样品 1 · Human CDAN1-interacting nuclease 1 (frames 692 - 701)

浓度— – 10.0 缓冲液 / pH20 mM Tris HCl, 150 mM NaCl, 5% glycerol / 8.0
实验温度20.0 设备 / 束线PETRA III / EMBL P12
波长0.123982 nm曝光0.495 s × 1200

分子组分

组分类型 / 物种UniProt 与构建体寡聚状态分子量
CDAN1-interacting nuclease 1
查看序列
SGTLPETGSSEAMILTKAQYDEIAQCLVSVPPTRQSLRKLKQRFPSQSQATLLSIFSQEYQKHIKRTHAKHHTSEAIESYYQRYLNGVVKNGAAPVLLDLANEVDYAPSLMARLILERFLQEHEETPPSKSIINSMLRDPSQIPDGVLANQVYQCIVNDCCYGPLVDCIKHAIGHEHEVLLRDLLLEKNLSFLDEDQLRAKGYDKTPDFILQVPVAVEGHIIHWIESKASFGDECSHHAYLHDQFWSYWNRFGPGLVIYWYGFIQELDCNRERGILLKACFPTNIVTLCHSIA
proteinHomo sapiensQ9Y2V01–281monomer分子数 133.381 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
11534[3]0.02595352–4.43393 1/nm含误差列缺失 0238sasbdb/entries/39/sasdv39/source/SASDV39.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)8.94—nm
i0Guinier2016.77—arbitrary
i0P(r)2022.08.77arbitrary
mwExperimental33.0—kDa
mwPorod62.0—kDa
porod_volumePorod104.0—nm³
rgGuinier2.810.033nm
rgP(r)2.8160.01nm

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20 mM Tris HCl, 150 mM NaCl, 5% glycerol缓冲液浓度—
pH8.0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2023-09-29储存 / 测量温度20.0 / 20.0
曝光时间0.495帧数1200
波长0.123982样品-探测器距离3.0
光源X-ray synchrotron探测器Pilatus 6M
机构 / 束线PETRA III / EMBL P12 · DESY; Hamburg, Germany
q 范围0.026 – 4.434样品体积 / 流速45.0 / 0.3

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/39/sasdv39/source/SASDV39.datdownloaded716111a218cdcdb0e175dd0312fa2dfa8b2116729f6199049c7c058218cdc1ad61eeb下载查看原文件源站
full_entry_zipsasbdb/entries/39/sasdv39/source/SASDV39.zipdownloaded346394581595b3129c90005f4ce9dd66be096b01ec3a399295a87b6d46613b782a070f下载查看原文件源站
pddfsasbdb/entries/39/sasdv39/source/SASDV39.outdownloaded859220354a3681aa8fcd32ffee2bacb251c3e10f457aded367e6b5b79c57f88735587下载查看原文件源站
sascifsasbdb/entries/39/sasdv39/source/SASDV39.sascifnot_available——下载查看原文件源站
summarysasbdb/entries/39/sasdv39/source/summary.jsondownloaded996040a5f56a44c3b4f4398dd2ef964fa041ac5e69b958edf994d4e64c496720a16f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:179 个字段值
字段路径原始值
codeSASDV39
statusPublished
type_of_curveSEC-SAS
angular_unit1/nm
project.titleAnemia-associated mutations disrupt the CDIN1-Codanin1 complex in inherited congenital dyserythropoietic anemia I (CDA-I) disease.
project.publication.titleAnemia-associated mutations disrupt the CDIN1-Codanin1 complex in inherited congenital dyserythropoietic anemia I (CDA-I) disease.
project.publication.author_listStojaspal M, Brom T, Nečasová I, Janovič T, Veverka P, Verma N, Uhrík L, Hernychova L, Hofr C
project.publication.journalFEBS J
project.publication.doi10.1111/febs.70421
project.publication.pmid41609415
project.publication.published_date2026 Jan 29
project.statusreleased
project.submitted_date2024-07-10
project.released_date2026-02-02
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intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDV39.dat
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sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDV39.sascif
experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus 6M
experiment.instrument.detector.resolutionnull
experiment.instrument.namePETRA III
experiment.instrument.cityDESY; Hamburg
experiment.instrument.countryGermany
experiment.instrument.beamline_nameEMBL P12
experiment.instrument.beam_geometrynull
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_nameCDAN1-interacting nuclease 1
experiment.sample.molecule[0].short_nameCDIN1
experiment.sample.molecule[0].sequenceSGTLPETGSSEAMILTKAQYDEIAQCLVSVPPTRQSLRKLKQRFPSQSQATLLSIFSQEYQKHIKRTHAKHHTSEAIESYYQRYLNGVVKNGAAPVLLDLANEVDYAPSLMARLILERFLQEHEETPPSKSIINSMLRDPSQIPDGVLANQVYQCIVNDCCYGPLVDCIKHAIGHEHEVLLRDLLLEKNLSFLDEDQLRAKGYDKTPDFILQVPVAVEGHIIHWIESKASFGDECSHHAYLHDQFWSYWNRFGPGLVIYWYGFIQELDCNRERGILLKACFPTNIVTLCHSIA
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeQ9Y2V0
experiment.sample.molecule[0].uniprot_range_first1
experiment.sample.molecule[0].uniprot_range_last281
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMILTKAQYDEIAQCLVSVPPTRQSLRKLKQRFPSQSQATLLSIFSQEYQKHIKRTHAKHH TSEAIESYYQRYLNGVVKNGAAPVLLDLANEVDYAPSLMARLILERFLQEHEETPPSKSI INSMLRDPSQIPDGVLANQVYQCIVNDCCYGPLVDCIKHAIGHEHEVLLRDLLLEKNLSF LDEDQLRAKGYDKTPDFILQVPVAVEGHIIHWIESKASFGDECSHHAYLHDQFWSYWNRF GPGLVIYWYGFIQELDCNRERGILLKACFPTNIVTLCHSIA
experiment.sample.molecule[0].mw33.381
experiment.sample.molecule[0].total_mw33.381
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_descriptionThe protein construct used for SAXS contains an additional 12 non-native amino acids at the N-terminus (SGTLPETGSSEA).
experiment.sample.buffer.name20 mM Tris HCl, 150 mM NaCl, 5% glycerol
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph8.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameHuman CDAN1-interacting nuclease 1 (frames 692 - 701)
experiment.sample.ext_coefficientnull
experiment.sample.contrastnull
experiment.sample.specific_volnull
experiment.sample.dry_volnull
experiment.sample.absorbptionnull
experiment.sample.deuterationnull
experiment.sample.mixturenull
experiment.contributor[0].affiliation[0].short_namenull
experiment.contributor[0].affiliation[0].addressnull
experiment.contributor[0].affiliation[0].full_nameNational Centre for Biomolecular Research, Faculty of Science, Masaryk University
experiment.contributor[0].affiliation[0].webpagenull
experiment.contributor[0].contributor_nameTomas
experiment.contributor[0].contributor_surnameBrom
experiment.contributor[0].orcidhttps://orcid.org/0000-0003-1046-192X
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2023-09-29
experiment.storage_temperature20.0
experiment.cell_temperature20.0
experiment.exposure_time0.495
experiment.number_of_frames1200
experiment.wavelength0.123982
experiment.sample_detector_distance3.0
experiment.concentration_minnull
experiment.concentration_max10.0
experiment.sample_volume45.0
experiment.flow_rate0.3
experiment.s_min0.026
experiment.s_max4.434
experiment.total_exposure_timenull
experiment.seccolumn2
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fits[0].models[0].softwareAlphaFold
fits[0].models[0].pdb_link[]
fits[0].models[0].model_titlenull
fits[0].models[0].type_of_modelatomic
fits[0].models[0].software_version2.0
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fits[0].models[0].model_mw66.74
fits[0].models[0].bead_radiusnull
fits[0].models[0].lognull
fits[0].models[0].symmetrynull
fits[0].models[0].commentnull
fits[0].models[0].user720
fits[0].fit_unit1/A
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fits[0].softwareCRYSOL
fits[0].chi_square_value1.063
fits[0].p_value0.3057
fits[0].fit_residual_plotSASDV39_fit1_fitresiduals_img.png
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fits[0].software_version3.2.1
fits[0].description
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fits[1].models[0].model_mw33.37
fits[1].models[0].bead_radiusnull
fits[1].models[0].lognull
fits[1].models[0].symmetrynull
fits[1].models[0].commentnull
fits[1].models[0].user720
fits[1].fit_unit1/A
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fits[1].softwareCRYSOL
fits[1].chi_square_value2.596
fits[1].p_value0.0
fits[1].fit_residual_plotSASDV39_fit2_fitresiduals_img.png
fits[1].fit_datahttps://www.sasbdb.org/media/fitting_files/SASDV39_fit2.FIT
fits[1].fit_loghttps://www.sasbdb.org/media/fitting_files/log_files/CHROMI1.LOG
fits[1].software_version3.2.1.
fits[1].description
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionThe SEC-SAXS data from the solution of CDIN1 diluted in 20 mM Tris HCl, 150 mM NaCl, 5% glycerol, pH 8.0 buffer were collected on the EMBL P12 beamline at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.123982 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAXS was employed. The sample (45 μl at 10 mg/ml) was injected and ran into a GE Superdex 200 Increase 5/150 column at a flow rate of 0.3 ml/min at 20°C. Scattering data were collected throughout the entire SEC column elution with an exposure time of 0.495 sec/frame (for 1200 frames total). The data were normalized to the intensity of the transmitted beam. The selected area of sample elution peak was selected and processed (averaged and buffer subtracted) from 10 data frames using CHROMIXS and primusqt from the ATSAS 3.2.1 package. The radius of gyration (Rg), forward scattering (I(0)), maximum particle dimension (Dmax), and the distance distribution function were determined using primusqt and GNOM. The calculated molecular weight (MW) of CDIN1 is around 67 kDa. MALDI-TOF mass spectrometry suggests a MW 33 369 Da for the CDIN1 monomer. The MW estimation from the SAXS data (primusqt) varied depending on the method used: Qp = 66.3 kDa, MoW = 62.3 kDa, Vc = 66.6 kDa, Size & Shape = 76.6 kDa (Bayesian Inference MW, 62.3 kDa in the 92% credibility interval of 58.8-67.9 kDa). The models displayed in this entry included: Top: The Alphafold2 predicted model of CDIN1 dimer compared with the SAXS data using CRYSOL. Bottom: The Alphafold2 predicted model of CDIN1 monomer compared with the SAXS data using CRYSOL.
tags[]
intensity_unitarbitrary
experimental_mw33.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw62.0
porod_mw_errornull
pddf_i02022.0
pddf_i0_error8.77
guinier_i02016.77
guinier_i0_errornull
pddf_rg2.816
pddf_rg_error0.01
guinier_rg2.81
guinier_rg_error0.033
pddf_dmax8.94
pddf_dmax_errornull
porod_volume104.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first45
guinier_point_last148
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDV39_datloglog_img.png
symmetrynull
last_modified2026-02-02T14:39:25.988588+01:00
bragg_peak[]
manifest.json:34 个字段值
字段路径原始值
codeSASDV39
statussuccess
started_at2026-08-11T16:38:33.687462+00:00
finished_at2026-08-11T16:38:42.059102+00:00
source_last_modified2026-02-02T14:39:25.988588+01:00
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查看完整 summary.json 原文
{
  "code": "SASDV39",
  "status": "Published",
  "type_of_curve": "SEC-SAS",
  "angular_unit": "1/nm",
  "project": {
    "title": "Anemia-associated mutations disrupt the CDIN1-Codanin1 complex in inherited congenital dyserythropoietic anemia I (CDA-I) disease.",
    "publication": {
      "title": "Anemia-associated mutations disrupt the CDIN1-Codanin1 complex in inherited congenital dyserythropoietic anemia I (CDA-I) disease.",
      "author_list": "Stojaspal M, Brom T, Nečasová I, Janovič T, Veverka P, Verma N, Uhrík L, Hernychova L, Hofr C",
      "journal": "FEBS J",
      "doi": "10.1111/febs.70421",
      "pmid": "41609415",
      "published_date": "2026 Jan 29"
    },
    "status": "released",
    "submitted_date": "2024-07-10",
    "released_date": "2026-02-02"
  },
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  "sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDV39.sascif",
  "experiment": {
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        "name": "Pilatus 6M",
        "resolution": null
      },
      "name": "PETRA III",
      "city": "DESY; Hamburg",
      "country": "Germany",
      "beamline_name": "EMBL P12",
      "beam_geometry": null,
      "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": "CDAN1-interacting nuclease 1",
          "short_name": "CDIN1",
          "sequence": "SGTLPETGSSEAMILTKAQYDEIAQCLVSVPPTRQSLRKLKQRFPSQSQATLLSIFSQEYQKHIKRTHAKHHTSEAIESYYQRYLNGVVKNGAAPVLLDLANEVDYAPSLMARLILERFLQEHEETPPSKSIINSMLRDPSQIPDGVLANQVYQCIVNDCCYGPLVDCIKHAIGHEHEVLLRDLLLEKNLSFLDEDQLRAKGYDKTPDFILQVPVAVEGHIIHWIESKASFGDECSHHAYLHDQFWSYWNRFGPGLVIYWYGFIQELDCNRERGILLKACFPTNIVTLCHSIA",
          "organism": "Homo sapiens",
          "uniprot_code": "Q9Y2V0",
          "uniprot_range_first": 1,
          "uniprot_range_last": 281,
          "oligomerization": "monomer",
          "molecular_type": "protein",
          "uniprot_sequence": "MILTKAQYDEIAQCLVSVPPTRQSLRKLKQRFPSQSQATLLSIFSQEYQKHIKRTHAKHH\nTSEAIESYYQRYLNGVVKNGAAPVLLDLANEVDYAPSLMARLILERFLQEHEETPPSKSI\nINSMLRDPSQIPDGVLANQVYQCIVNDCCYGPLVDCIKHAIGHEHEVLLRDLLLEKNLSF\nLDEDQLRAKGYDKTPDFILQVPVAVEGHIIHWIESKASFGDECSHHAYLHDQFWSYWNRF\nGPGLVIYWYGFIQELDCNRERGILLKACFPTNIVTLCHSIA",
          "mw": 33.381,
          "total_mw": 33.381,
          "number_molecules": 1,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": "The protein construct used for SAXS contains an additional 12 non-native amino acids at the N-terminus (SGTLPETGSSEA)."
        }
      ],
      "buffer": {
        "name": "20 mM Tris HCl, 150 mM NaCl, 5% glycerol",
        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 8.0,
        "deuteration": null
      },
      "purity_method": null,
      "name": "Human CDAN1-interacting nuclease 1 (frames 692 - 701)",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": null,
            "address": null,
            "full_name": "National Centre for Biomolecular Research, Faculty of Science, Masaryk University",
            "webpage": null
          }
        ],
        "contributor_name": "Tomas",
        "contributor_surname": "Brom",
        "orcid": "https://orcid.org/0000-0003-1046-192X"
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2023-09-29",
    "storage_temperature": 20.0,
    "cell_temperature": 20.0,
    "exposure_time": 0.495,
    "number_of_frames": 1200,
    "wavelength": 0.123982,
    "sample_detector_distance": 3.0,
    "concentration_min": null,
    "concentration_max": 10.0,
    "sample_volume": 45.0,
    "flow_rate": 0.3,
    "s_min": 0.026,
    "s_max": 4.434,
    "total_exposure_time": null,
    "seccolumn": 2
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  "fits": [
    {
      "models": [
        {
          "model_plot": "https://www.sasbdb.org/media/pdb_file/images/SASDV39_fit1_model1_img.png",
          "software": "AlphaFold",
          "pdb_link": [],
          "model_title": null,
          "type_of_model": "atomic",
          "software_version": "2.0",
          "model_data": "https://www.sasbdb.org/media/pdb_file/SASDV39_fit1_model1.pdb",
          "model_mw": 66.74,
          "bead_radius": null,
          "log": null,
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          "user": 720
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      "fit_unit": "1/A",
      "fit_plot": "https://www.sasbdb.org/media/fitting_files/scattering_plots/SASDV39_fit1_fixed_fit_img.png",
      "software": "CRYSOL",
      "chi_square_value": 1.063,
      "p_value": 0.3057,
      "fit_residual_plot": "SASDV39_fit1_fitresiduals_img.png",
      "fit_data": "https://www.sasbdb.org/media/fitting_files/SASDV39_fit1.FIT",
      "fit_log": "https://www.sasbdb.org/media/fitting_files/log_files/CHROMI2.LOG",
      "software_version": "3.2.1",
      "description": ""
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    {
      "models": [
        {
          "model_plot": "https://www.sasbdb.org/media/pdb_file/images/SASDV39_fit2_model1_img.png",
          "software": "AlphaFold",
          "pdb_link": [],
          "model_title": null,
          "type_of_model": "atomic",
          "software_version": "2.0",
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      "software": "CRYSOL",
      "chi_square_value": 2.596,
      "p_value": 0.0,
      "fit_residual_plot": "SASDV39_fit2_fitresiduals_img.png",
      "fit_data": "https://www.sasbdb.org/media/fitting_files/SASDV39_fit2.FIT",
      "fit_log": "https://www.sasbdb.org/media/fitting_files/log_files/CHROMI1.LOG",
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  "pddf_software": "ATSAS GNOM",
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  "i0_calibration_standard": null,
  "description": null,
  "experiment_description": "The SEC-SAXS data from the solution of CDIN1 diluted in 20 mM Tris HCl, 150 mM NaCl, 5% glycerol, pH 8.0 buffer were collected on the EMBL P12 beamline at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.123982 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAXS was employed. The sample (45 μl at 10 mg/ml) was injected and ran into a GE Superdex 200 Increase 5/150 column at a flow rate of 0.3 ml/min at 20°C. Scattering data were collected throughout the entire SEC column elution with an exposure time of 0.495 sec/frame (for 1200 frames total). The data were normalized to the intensity of the transmitted beam. The selected area of sample elution peak was selected and processed (averaged and buffer subtracted) from 10 data frames using CHROMIXS and primusqt from the ATSAS 3.2.1 package. The radius of gyration (Rg), forward scattering (I(0)), maximum particle dimension (Dmax), and the distance distribution function were determined using primusqt and GNOM. The calculated molecular weight (MW) of CDIN1 is around 67 kDa. MALDI-TOF mass spectrometry suggests a MW 33 369 Da for the CDIN1 monomer. The MW estimation from the SAXS data (primusqt) varied depending on the method used: Qp = 66.3 kDa, MoW = 62.3 kDa, Vc = 66.6 kDa, Size & Shape = 76.6 kDa (Bayesian Inference MW, 62.3 kDa in the 92% credibility interval of 58.8-67.9 kDa). The models displayed in this entry included: Top: The Alphafold2 predicted model of CDIN1 dimer compared with the SAXS data using CRYSOL. Bottom: The Alphafold2 predicted model of CDIN1 monomer compared with the SAXS data using CRYSOL.",
  "tags": [],
  "intensity_unit": "arbitrary",
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  "guinier_rg_error": 0.033,
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  "porod_volume": 104.0,
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  "guinier_point_first": 45,
  "guinier_point_last": 148,
  "pddf_point_first": null,
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  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDV39_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2026-02-02T14:39:25.988588+01:00",
  "bragg_peak": []
}
查看完整 manifest.json 原文
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