SASDF52

dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Single concentration 最后更新:2020-08-28T15:27:32.015613+02:00

Construct contains an additional two amino acids (Gly-Ala) at the N-terminus as a remaining product the TEV-protease cleavage. The data displayed in this entry consists of merged data from three replicates of equal sample concentration (5.0 mg/ml). Thus, an effective total of 30 frames x 1s exposures is collated for this curve. The data were merged using Primus and datmerge of the ATSAS 2.8.4-1 package maintained by SBGrid.

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1. 样品、组分与实验条件 Sample & Experiment

样品 1 · dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE

浓度5.0 – 5.0 缓冲液 / pH20 mM NaPO4, 200 mM NaCl, 1 mM DTT / 6.5
实验温度20.0 设备 / 束线ESRF / BM29
波长0.09919 nm曝光1.0 s × 10

分子组分

组分类型 / 物种UniProt 与构建体寡聚状态分子量
Dosage compensation regulator
查看序列
>DSRBD12_SINGLE|CHAINA|259AAGAMDIKSFLYQFCAKSQIEPKFDIRQTGPKNRQRFLCEVRVEPNTYIGVGNSTNKKDAEKNACRDFVNYLVRVGKLNTNDVPADAGASGGGPRTGLEGAGMAGGSGQQKRVFDGQSGPQDLGEAYRPLNHDGGDGGNRYSVIDRIQEQRDMNEAEAFDVNAAIHGNWTIENAKERLNIYKQTNNIRDDYKYTPVGPEHARSFLAELSIYVPALNRTVTARESGSNKKSASKSCALSLVRQLFHLNVIEPFSGTLKKKKD
proteinDrosophila melanogasterP247851–257monomer分子数 128.549 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
11043[3]0.03479421–4.943923 1/nm含误差列缺失 00sasbdb/entries/52/sasdf52/source/SASDF52.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)12.5—nm
i0Guinier66.260.13arbitrary
i0P(r)66.44—arbitrary
mwExperimental14.8—kDa
mwPorod14.0—kDa
porod_volumePorod22.0—nm³
rgGuinier3.230.13nm
rgP(r)3.337—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

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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 NaPO4, 200 mM NaCl, 1 mM DTT缓冲液浓度—
pH6.5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2016-11-29储存 / 测量温度— / 20.0
曝光时间1.0帧数10
波长0.09919样品-探测器距离2.867
光源X-ray synchrotron探测器Pilatus 1M
机构 / 束线ESRF / BM29 · Grenoble, France
q 范围0.035 – 4.944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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curve:来源记录
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full_entry_zip:来源记录与 ZIP 内部目录(8 项)
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pddf: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:195 个字段值
字段路径原始值
codeSASDF52
statusPublished
type_of_curveSingle concentration
angular_unit1/nm
project.titleStructure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless.
project.publication.titleStructure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless.
project.publication.author_listAnkush Jagtap PK, Müller M, Masiewicz P, von Bülow S, Hollmann NM, Chen PC, Simon B, Thomae AW, Becker PB, Hennig J
project.publication.journalNucleic Acids Res
project.publication.doi10.1093/nar/gkz125
project.publication.pmid30805612
project.publication.published_date2019 May 7
project.statusreleased
project.submitted_date2019-01-28
project.released_date2019-02-21
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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_nameDosage compensation regulator
experiment.sample.molecule[0].short_nameMLE
experiment.sample.molecule[0].sequence> dsRBD12_single | chain A | 259 aa GAMDIKSFLYQFCAKSQIEPKFDIRQTGPKNRQRFLCEVRVEPNTYIGVGNSTNKKDAEK NACRDFVNYLVRVGKLNTNDVPADAGASGGGPRTGLEGAGMAGGSGQQKRVFDGQSGPQD LGEAYRPLNHDGGDGGNRYSVIDRIQEQRDMNEAEAFDVNAAIHGNWTIENAKERLNIYK QTNNIRDDYKYTPVGPEHARSFLAELSIYVPALNRTVTARESGSNKKSASKSCALSLVRQ LFHLNVIEPFSGTLKKKKD
experiment.sample.molecule[0].organismDrosophila melanogaster
experiment.sample.molecule[0].uniprot_codeP24785
experiment.sample.molecule[0].uniprot_range_first1
experiment.sample.molecule[0].uniprot_range_last257
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMDIKSFLYQFCAKSQIEPKFDIRQTGPKNRQRFLCEVRVEPNTYIGVGNSTNKKDAEKNA CRDFVNYLVRVGKLNTNDVPADAGASGGGPRTGLEGAGMAGGSGQQKRVFDGQSGPQDLG EAYRPLNHDGGDGGNRYSVIDRIQEQRDMNEAEAFDVNAAIHGNWTIENAKERLNIYKQT NNIRDDYKYTPVGPEHARSFLAELSIYVPALNRTVTARESGSNKKSASKSCALSLVRQLF HLNVIEPFSGTLKKKKDEQLKPYPVKLSPNLINKIDEVIKGLDLPVVNPRNIKIELDGPP IPLIVNLSRIDSSQQDGEKRQESSVIPWAPPQANWNTWHACNIDEGELATTSIDDLSMDY ERSLRDRRQNDNEYRQFLEFREKLPIAAMRSEILTAINDNPVVIIRGNTGCGKTTQIAQY ILDDYICSGQGGYANIYVTQPRRISAISVAERVARERCEQLGDTVGYSVRFESVFPRPYG AILFCTVGVLLRKLEAGLRGVSHIIVDEIHERDVNSDFLLVILRDMVDTYPDLHVILMSA TIDTTKFSKYFGICPVLEVPGRAFPVQQFFLEDIIQMTDFVPSAESRRKRKEVEDEEQLL SEDKDEAEINYNKVCEDKYSQKTRNAMAMLSESDVSFELLEALLMHIKSKNIPGAILVFL PGWNLIFALMKFLQNTNIFGDTSQYQILPCHSQIPRDEQRKVFEPVPEGVTKIILSTNIA ETSITIDDIVFVIDICKARMKLFTSHNNLTSYATVWASKTNLEQRKGRAGRVRPGFCFTL CSRARFQALEDNLTPEMFRTPLHEMALTIKLLRLGSIHHFLSKALEPPPVDAVIEAEVLL REMRCLDANDELTPLGRLLARLPIEPRLGKMMVLGAVFGCADLMAIMASYSSTFSEVFSL DIGQRRLANHQKALSGTKCSDHVAMIVASQMWRREKQRGEHMEARFCDWKGLQMSTMNVI WDAKQQLLDLLQQAGFPEECMISHEVDERIDGDDPVLDVSLALLCLGLYPNICVHKEKRK VLTTESKAALLHKTSVNCSNLAVTFPYPFFVFGEKIRTRAVSCKQLSMVSPLQVILFGSR KIDLAANNIVRVDNWLNFDIEPELAAKIGALKPALEDLITVACDNPSDILRLEEPYAQLV KVVKDLCVKSAGDFGLQRESGILPHQSRQFSDGGGPPKRGRFETGRFTNSSFGRRGNGRT FGGGYGNNGGGYGNNGGGYGNIGGGYGNNAGGYGNNGGYGNNGGGYRNNGGGYGNNGGGY GNKRGGFGDSFESNRGSGGGFRNGDQGGRWGNF
experiment.sample.molecule[0].mw28.549
experiment.sample.molecule[0].total_mw28.549
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_descriptionnull
experiment.sample.buffer.name20 mM NaPO4, 200 mM NaCl, 1 mM DTT
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph6.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.namedsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE
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_nameEMBL
experiment.contributor[0].affiliation[0].addressHeidelberg, Germany
experiment.contributor[0].affiliation[0].full_nameEuropean Molecular Biology Laboratory (EMBL) - Heidelberg
experiment.contributor[0].affiliation[0].webpagehttps://www.embl.de/
experiment.contributor[0].contributor_namePo-chia
experiment.contributor[0].contributor_surnameChen
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2016-11-29
experiment.storage_temperaturenull
experiment.cell_temperature20.0
experiment.exposure_time1.0
experiment.number_of_frames10
experiment.wavelength0.09919
experiment.sample_detector_distance2.867
experiment.concentration_min5.0
experiment.concentration_max5.0
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experiment.flow_ratenull
experiment.s_min0.035
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experiment.seccolumnnull
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fits[0].chi_square_value2.089
fits[0].p_value0.0
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fits[0].description
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionConstruct contains an additional two amino acids (Gly-Ala) at the N-terminus as a remaining product the TEV-protease cleavage. The data displayed in this entry consists of merged data from three replicates of equal sample concentration (5.0 mg/ml). Thus, an effective total of 30 frames x 1s exposures is collated for this curve. The data were merged using Primus and datmerge of the ATSAS 2.8.4-1 package maintained by SBGrid.
experiment_descriptionSynchrotron SAXS data from solutions of the dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE, in 20 mM NaPO4, 200 mM NaCl, 1 mM DTT, pH 6.5 were collected 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 = 0.09919 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). A solute concentration of 5 mg/ml was measured at 20°C. 10 successive 1 second frames were collected per sample (three replicates total). The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
tags[]
intensity_unitarbitrary
experimental_mw14.8
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw14.0
porod_mw_errornull
pddf_i066.44
pddf_i0_errornull
guinier_i066.26
guinier_i0_error0.13
pddf_rg3.337
pddf_rg_errornull
guinier_rg3.23
guinier_rg_error0.13
pddf_dmax12.5
pddf_dmax_errornull
porod_volume22.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first6
guinier_point_last60
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDF52_datloglog_img.png
symmetrynull
last_modified2020-08-28T15:27:32.015613+02:00
bragg_peak[]
manifest.json:36 个字段值
字段路径原始值
codeSASDF52
statussuccess
started_at2026-08-11T13:30:39.696317+00:00
finished_at2026-08-11T13:30:48.798979+00:00
source_last_modified2020-08-28T15:27:32.015613+02:00
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查看完整 summary.json 原文
{
  "code": "SASDF52",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/nm",
  "project": {
    "title": "Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless.",
    "publication": {
      "title": "Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless.",
      "author_list": "Ankush Jagtap PK, Müller M, Masiewicz P, von Bülow S, Hollmann NM, Chen PC, Simon B, Thomae AW, Becker PB, Hennig J",
      "journal": "Nucleic Acids Res",
      "doi": "10.1093/nar/gkz125",
      "pmid": "30805612",
      "published_date": "2019 May 7"
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    "status": "released",
    "submitted_date": "2019-01-28",
    "released_date": "2019-02-21"
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      "country": "France",
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            "short_name": "EMBL",
            "address": "Heidelberg, Germany",
            "full_name": "European Molecular Biology Laboratory (EMBL) - Heidelberg",
            "webpage": "https://www.embl.de/"
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}
查看完整 manifest.json 原文
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