SASDFX3

Semi-synthetic nucleosome core particle (NCP)

数据类型:SASBDB 实验数据 状态:Published 曲线类型:SEC-SAS 最后更新:2019-12-06T13:07:15.624532+01:00
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1. 样品、组分与实验条件 Sample & Experiment

样品 1 · Semi-synthetic nucleosome core particle (NCP)

浓度— – 1.8 缓冲液 / pH15 mM HEPES, 200 mM NaCl / 7.3
实验温度20.0 设备 / 束线ESRF / BM29
波长0.1 nm曝光1.0 s × 243

分子组分

组分类型 / 物种UniProt 与构建体寡聚状态分子量
Histone H3
查看序列
ARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
proteinXenopus laevis—2–136dimer分子数 215.271 kDa
Histone H4
查看序列
SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
proteinXenopus laevisP627992–103dimer分子数 211.236 kDa
Histone H2a
查看序列
SGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKTESSKSAKSK
proteinXenopus laevisQ6AZJ82–130dimer分子数 213.95 kDa
Histone H2b
查看序列
AKSAPAPKKGSKKAVTKTQKKDGKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK
proteinXenopus laevisQ921305–126dimer分子数 213.494 kDa
147bp 601 Widom sequence
查看序列
ATCGAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAAACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCAGGCACGTGTCAGATATATACATCCGAT
DNAsynthetic construct——–—monomer分子数 145.202 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
1593[3]0.07138524–2.852432 1/nm含误差列缺失 05sasbdb/entries/x3/sasdfx3/source/SASDFX3.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)12.8—nm
i0Guinier91.260.1arbitrary
i0P(r)90.55—arbitrary
mwExperimental200.0—kDa
porod_volumePorod353.0—nm³
rgGuinier4.350.01nm
rgP(r)4.268—nm

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

该条目没有来源拟合记录。

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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15 mM HEPES, 200 mM NaCl缓冲液浓度—
pH7.3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2017-12-11储存 / 测量温度4.0 / 20.0
曝光时间1.0帧数243
波长0.1样品-探测器距离2.87
光源X-ray synchrotron探测器Pilatus 1M
机构 / 束线ESRF / BM29 · Grenoble, France
q 范围0.071 – 2.852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/x3/sasdfx3/source/SASDFX3.zipdownloaded19514609558a4eb9a08f5126c676304cfb300bb98ced8082c2df2973f831423d72094下载查看原文件源站
pddfsasbdb/entries/x3/sasdfx3/source/SASDFX3.outdownloaded38485b7a2067ce13ace7d5c6d8b35f280808c005dd624726889910f9d777030324a07下载查看原文件源站
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summarysasbdb/entries/x3/sasdfx3/source/summary.jsondownloaded96646d6817c1a2d1580299808a0dd163d43096c09f8ff5917a473dc371c2c46c6083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(2 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:202 个字段值
字段路径原始值
codeSASDFX3
statusPublished
type_of_curveSEC-SAS
angular_unit1/nm
project.titleA Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC Multimeric Complex.
project.publication.titleA Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC Multimeric Complex.
project.publication.author_listMarabelli C, Marrocco B, Pilotto S, Chittori S, Picaud S, Marchese S, Ciossani G, Forneris F, Filippakopoulos P, Schoehn G, Rhodes D, Subramaniam S, Mattevi A
project.publication.journalCell Rep
project.publication.doi10.1016/j.celrep.2019.03.061
project.publication.pmid30970244
project.publication.published_date2019 Apr 9
project.statusreleased
project.submitted_date2019-03-12
project.released_date2019-04-16
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDFX3.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDFX3.dat
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intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDFX3_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDFX3.sascif
experiment.instrument.detector.typeDectris
experiment.instrument.detector.namePilatus 1M
experiment.instrument.detector.resolution172.0
experiment.instrument.nameESRF
experiment.instrument.cityGrenoble
experiment.instrument.countryFrance
experiment.instrument.beamline_nameBM29
experiment.instrument.beam_geometry
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_nameHistone H3
experiment.sample.molecule[0].short_nameH3
experiment.sample.molecule[0].sequenceARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQR LVREIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
experiment.sample.molecule[0].organismXenopus laevis
experiment.sample.molecule[0].uniprot_codenull
experiment.sample.molecule[0].uniprot_range_first2
experiment.sample.molecule[0].uniprot_range_last136
experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequencenull
experiment.sample.molecule[0].mw15.271
experiment.sample.molecule[0].total_mw30.542
experiment.sample.molecule[0].number_molecules2
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_nameHistone H4
experiment.sample.molecule[1].short_nameH4
experiment.sample.molecule[1].sequenceSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDA VTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
experiment.sample.molecule[1].organismXenopus laevis
experiment.sample.molecule[1].uniprot_codeP62799
experiment.sample.molecule[1].uniprot_range_first2
experiment.sample.molecule[1].uniprot_range_last103
experiment.sample.molecule[1].oligomerizationdimer
experiment.sample.molecule[1].molecular_typeprotein
experiment.sample.molecule[1].uniprot_sequenceMSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLK VFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
experiment.sample.molecule[1].mw11.236
experiment.sample.molecule[1].total_mw22.472
experiment.sample.molecule[1].number_molecules2
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.molecule[2].long_nameHistone H2a
experiment.sample.molecule[2].short_nameH2a
experiment.sample.molecule[2].sequenceSGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNA ARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKTESSKSAKSK
experiment.sample.molecule[2].organismXenopus laevis
experiment.sample.molecule[2].uniprot_codeQ6AZJ8
experiment.sample.molecule[2].uniprot_range_first2
experiment.sample.molecule[2].uniprot_range_last130
experiment.sample.molecule[2].oligomerizationdimer
experiment.sample.molecule[2].molecular_typeprotein
experiment.sample.molecule[2].uniprot_sequenceMSGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLT AEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKK TESSKSAKSK
experiment.sample.molecule[2].mw13.95
experiment.sample.molecule[2].total_mw27.9
experiment.sample.molecule[2].number_molecules2
experiment.sample.molecule[2].complex_stateFalse
experiment.sample.molecule[2].deuterationnull
experiment.sample.molecule[2].molecule_sourcebiological
experiment.sample.molecule[2].molecule_descriptionnull
experiment.sample.molecule[3].long_nameHistone H2b
experiment.sample.molecule[3].short_nameH2b
experiment.sample.molecule[3].sequenceAKSAPAPKKGSKKAVTKTQKKDGKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFER IAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK
experiment.sample.molecule[3].organismXenopus laevis
experiment.sample.molecule[3].uniprot_codeQ92130
experiment.sample.molecule[3].uniprot_range_first5
experiment.sample.molecule[3].uniprot_range_last126
experiment.sample.molecule[3].oligomerizationdimer
experiment.sample.molecule[3].molecular_typeprotein
experiment.sample.molecule[3].uniprot_sequenceMPDPAKSAPAAKKGSKKAVTKTQKKDGKKRRKSRKESYAIYVYKVLKQVHPDTGISSKAM SIMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVT KYTSAK
experiment.sample.molecule[3].mw13.494
experiment.sample.molecule[3].total_mw26.988
experiment.sample.molecule[3].number_molecules2
experiment.sample.molecule[3].complex_stateFalse
experiment.sample.molecule[3].deuterationnull
experiment.sample.molecule[3].molecule_sourcebiological
experiment.sample.molecule[3].molecule_descriptionnull
experiment.sample.molecule[4].long_name147bp 601 Widom sequence
experiment.sample.molecule[4].short_name601-147bp
experiment.sample.molecule[4].sequenceATCGAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAAACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCAGGCACGTGTCAGATATATACATCCGAT
experiment.sample.molecule[4].organismsynthetic construct
experiment.sample.molecule[4].uniprot_codenull
experiment.sample.molecule[4].uniprot_range_firstnull
experiment.sample.molecule[4].uniprot_range_lastnull
experiment.sample.molecule[4].oligomerizationmonomer
experiment.sample.molecule[4].molecular_typeDNA
experiment.sample.molecule[4].uniprot_sequencenull
experiment.sample.molecule[4].mw45.202
experiment.sample.molecule[4].total_mw45.202
experiment.sample.molecule[4].number_molecules1
experiment.sample.molecule[4].complex_stateFalse
experiment.sample.molecule[4].deuterationnull
experiment.sample.molecule[4].molecule_sourcebiological
experiment.sample.molecule[4].molecule_descriptionnull
experiment.sample.buffer.name15 mM HEPES, 200 mM 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.ph7.3
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameSemi-synthetic nucleosome core particle (NCP)
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].addressItaly
experiment.contributor[0].affiliation[0].full_nameUniversity of Pavia
experiment.contributor[0].affiliation[0].webpagehttp://wcm-3.unipv.it
experiment.contributor[0].contributor_nameFederico
experiment.contributor[0].contributor_surnameForneris
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2017-12-11
experiment.storage_temperature4.0
experiment.cell_temperature20.0
experiment.exposure_time1.0
experiment.number_of_frames243
experiment.wavelength0.1
experiment.sample_detector_distance2.87
experiment.concentration_minnull
experiment.concentration_max1.8
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.071
experiment.s_max2.852
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from solutions of a semi-synthetic nucleosome core particle (NCP) in 15 mM HEPES, 200 mM NaCl, pH 7.3 were collected using size-exclusion chromatography SAXS (SEC-SAXS) on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). SEC-SAXS was performed at 20 °C using the following parameters: Column: Wyatt WTC-030N5; Flow rate: 0.25 mL/min; Sample injection concentration: 2.5 mg/mL; Injection volume: 50 μL. The data were collected through the SEC peak of the sample as a series of 243 x 1 second exposures. Each unsubtracted data frame was normalised to the intensity of the transmitted beam and radially averaged and the scattering of an appropriate solvent-blank was subtracted. The resulting subtracted frames were scaled and averaged to generate the final SAXS profile displayed in this entry.
tags[]
intensity_unitarbitrary
experimental_mw200.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i090.55
pddf_i0_errornull
guinier_i091.26
guinier_i0_error0.1
pddf_rg4.268
pddf_rg_errornull
guinier_rg4.35
guinier_rg_error0.01
pddf_dmax12.8
pddf_dmax_errornull
porod_volume353.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first15
guinier_point_last56
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDFX3_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 个字段值
字段路径原始值
codeSASDFX3
statussuccess
started_at2026-08-11T14:10:07.228570+00:00
finished_at2026-08-11T14:10:15.193773+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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查看完整 summary.json 原文
{
  "code": "SASDFX3",
  "status": "Published",
  "type_of_curve": "SEC-SAS",
  "angular_unit": "1/nm",
  "project": {
    "title": "A Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC Multimeric Complex.",
    "publication": {
      "title": "A Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC Multimeric Complex.",
      "author_list": "Marabelli C, Marrocco B, Pilotto S, Chittori S, Picaud S, Marchese S, Ciossani G, Forneris F, Filippakopoulos P, Schoehn G, Rhodes D, Subramaniam S, Mattevi A",
      "journal": "Cell Rep",
      "doi": "10.1016/j.celrep.2019.03.061",
      "pmid": "30970244",
      "published_date": "2019 Apr 9"
    },
    "status": "released",
    "submitted_date": "2019-03-12",
    "released_date": "2019-04-16"
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            "address": "Italy",
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}
查看完整 manifest.json 原文
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