SASDF56

DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 4.5 with 150 mM NaCl

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Single concentration 最后更新:2020-06-22T11:01:44.799841+02:00

SAXS profile corresponds to a protein-DNA complex between bacterial nucleoid associated protein HUalpha and 80bp DNA. Under these conditions, the complex forms lamellar structures visible as Bragg Diffraction peaks.

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1. 样品、组分与实验条件 Sample & Experiment

样品 1 · DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 4.5 with 150 mM NaCl

浓度— – — 缓冲液 / pH10 mM sodium acetate, 150 mM NaCl / 4.5
实验温度10.0 设备 / 束线Advanced Light Source (ALS) / 12.3.1 (SIBYLS)
波长0.103 nm曝光3.0 s × 300

分子组分

组分类型 / 物种UniProt 与构建体寡聚状态分子量
80bp_DNA Forward
查看序列
AATGAGGTAACAACGAAAGCAGATGATAGCTGCTTATCAATTTGTTGCAAACAAGTAGCCGCGCCCAATGAGGTAACAAT
DNAEscherichia coli——–—monomer分子数 124.849 kDa
80bp_DNA Reverse
查看序列
TTACTCCATTGTTGCTTTCGTCTACTATCGACGAATAGTTAAACAACGTTTGTTCATCGGCGCGGGTTACTCCATTGTTA
DNAEscherichia coli——–—monomer分子数 124.612 kDa
DNA-binding protein HU-alpha
查看序列
MNKTQLIDVIAEKAELSKTQAKAALESTLAAITESLKEGDAVQLVGFGTFKVNHRAERTGRNPQTGKEIKIAAANVPAFVSGKALKDAVK
proteinEscherichia coliP0ACF01–90unknown分子数 —9.535 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
1608[3]0.011985–0.3503 1/A含误差列缺失 00sasbdb/entries/56/sasdf56/source/SASDF56.dat
▼

2. SASBDB 报告的指标 Reported Results

指标方法数值误差单位
mwExperimental350.0—kDa
rgP(r)2.0—Å

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10 mM sodium acetate, 150 mM NaCl缓冲液浓度—
pH4.5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2018-06-01储存 / 测量温度— / 10.0
曝光时间3.0帧数300
波长0.103样品-探测器距离1.5
光源X-ray synchrotron探测器Pilatus3 X 2M
机构 / 束线Advanced Light Source (ALS) / 12.3.1 (SIBYLS) · Berkeley, CA, USA
q 范围0.12 – 3.503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

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/56/sasdf56/source/SASDF56.zipdownloaded7451a2a72a02a2cb8199d53e721da8dcd950dc6135ed4b30378edb7846836aa09474下载查看原文件源站
pddfsasbdb/entries/56/sasdf56/source/SASDF56.outnot_listed——下载查看原文件
sascifsasbdb/entries/56/sasdf56/source/SASDF56.sascifdownloaded38361217da606f1ce25e42594b688af833f5ce123770c570359c487467b3bfeffd726下载查看原文件源站
summarysasbdb/entries/56/sasdf56/source/summary.jsondownloaded7553569c275f4dc2d0050ea85a9fb1f2b6f968eec20a75dde5577b21e2059f613e26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(1 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:168 个字段值
字段路径原始值
codeSASDF56
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleNucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling.
project.publication.titleNucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling.
project.publication.author_listRemesh SG, Verma SC, Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
project.publication.journalNat Commun
project.publication.doi10.1038/s41467-020-16724-5
project.publication.pmid32518228
project.publication.published_date2020 Jun 9
project.statusreleased
project.submitted_date2019-04-26
project.released_date2020-04-21
pddf_datanull
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDF56.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDF56_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDF56_kratky_img.png
pddf_plotnull
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDF56_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDF56.sascif
experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus3 X 2M
experiment.instrument.detector.resolution172.0
experiment.instrument.nameAdvanced Light Source (ALS)
experiment.instrument.cityBerkeley, CA
experiment.instrument.countryUSA
experiment.instrument.beamline_name12.3.1 (SIBYLS)
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_name80bp_DNA Forward
experiment.sample.molecule[0].short_namenull
experiment.sample.molecule[0].sequenceAATGAGGTAACAACGAAAGCAGATGATAGCTGCTTATCAATTTGTTGCAAACAAGTAGCCGCGCCCAATGAGGTAACAAT
experiment.sample.molecule[0].organismEscherichia coli
experiment.sample.molecule[0].uniprot_codenull
experiment.sample.molecule[0].uniprot_range_firstnull
experiment.sample.molecule[0].uniprot_range_lastnull
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeDNA
experiment.sample.molecule[0].uniprot_sequencenull
experiment.sample.molecule[0].mw24.849
experiment.sample.molecule[0].total_mw24.849
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.molecule[1].long_name80bp_DNA Reverse
experiment.sample.molecule[1].short_namenull
experiment.sample.molecule[1].sequenceTTACTCCATTGTTGCTTTCGTCTACTATCGACGAATAGTTAAACAACGTTTGTTCATCGGCGCGGGTTACTCCATTGTTA
experiment.sample.molecule[1].organismEscherichia coli
experiment.sample.molecule[1].uniprot_codenull
experiment.sample.molecule[1].uniprot_range_firstnull
experiment.sample.molecule[1].uniprot_range_lastnull
experiment.sample.molecule[1].oligomerizationmonomer
experiment.sample.molecule[1].molecular_typeDNA
experiment.sample.molecule[1].uniprot_sequencenull
experiment.sample.molecule[1].mw24.612
experiment.sample.molecule[1].total_mw24.612
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.molecule[2].long_nameDNA-binding protein HU-alpha
experiment.sample.molecule[2].short_namenull
experiment.sample.molecule[2].sequenceMNKTQLIDVIAEKAELSKTQAKAALESTLAAITESLKEGDAVQLVGFGTFKVNHRAERTGRNPQTGKEIKIAAANVPAFVSGKALKDAVK
experiment.sample.molecule[2].organismEscherichia coli
experiment.sample.molecule[2].uniprot_codeP0ACF0
experiment.sample.molecule[2].uniprot_range_first1
experiment.sample.molecule[2].uniprot_range_last90
experiment.sample.molecule[2].oligomerizationunknown
experiment.sample.molecule[2].molecular_typeprotein
experiment.sample.molecule[2].uniprot_sequenceMNKTQLIDVIAEKAELSKTQAKAALESTLAAITESLKEGDAVQLVGFGTFKVNHRAERTG RNPQTGKEIKIAAANVPAFVSGKALKDAVK
experiment.sample.molecule[2].mw9.535
experiment.sample.molecule[2].total_mw9.535
experiment.sample.molecule[2].number_molecules0
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.buffer.name10 mM sodium acetate, 150 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.ph4.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameDNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 4.5 with 150 mM NaCl
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_nameUCSF
experiment.contributor[0].affiliation[0].addressSan Francisco, CA, USA
experiment.contributor[0].affiliation[0].full_nameUniversity of California, San Francisco (UCSF)
experiment.contributor[0].affiliation[0].webpagehttps://www.ucsf.edu/
experiment.contributor[0].contributor_nameSoumya
experiment.contributor[0].contributor_surnameG Remesh
experiment.contributor[0].orcid
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2018-06-01
experiment.storage_temperaturenull
experiment.cell_temperature10.0
experiment.exposure_time3.0
experiment.number_of_frames300
experiment.wavelength0.103
experiment.sample_detector_distance1.5
experiment.concentration_minnull
experiment.concentration_maxnull
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.12
experiment.s_max3.503
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwarenull
pddf_software_versionnull
i0_calibration_standardnull
descriptionSAXS profile corresponds to a protein-DNA complex between bacterial nucleoid associated protein HUalpha and 80bp DNA. Under these conditions, the complex forms lamellar structures visible as Bragg Diffraction peaks.
experiment_descriptionSynchrotron SAXS data from solutions of DNA-binding protein HU-alpha bound to 80 base-pair DNA in 10 mM sodium acetate, 150 mM NaCl, pH 4.5 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS) storage ring (Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.103 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). 300 successive 3 second frames were collected at 10°C. 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_mw350.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i0null
pddf_i0_errornull
guinier_i0null
guinier_i0_errornull
pddf_rg2.0
pddf_rg_errornull
guinier_rgnull
guinier_rg_errornull
pddf_dmaxnull
pddf_dmax_errornull
porod_volumenull
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_plotSASDF56_datloglog_img.png
symmetrynull
last_modified2020-06-22T11:01:44.799841+02:00
bragg_peak[]
manifest.json:33 个字段值
字段路径原始值
codeSASDF56
statussuccess
started_at2026-08-11T16:48:19.847649+00:00
finished_at2026-08-11T16:48:25.331053+00:00
source_last_modified2020-06-22T11:01:44.799841+02:00
files[0].statusdownloaded
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查看完整 summary.json 原文
{
  "code": "SASDF56",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling.",
    "publication": {
      "title": "Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling.",
      "author_list": "Remesh SG, Verma SC, Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M",
      "journal": "Nat Commun",
      "doi": "10.1038/s41467-020-16724-5",
      "pmid": "32518228",
      "published_date": "2020 Jun 9"
    },
    "status": "released",
    "submitted_date": "2019-04-26",
    "released_date": "2020-04-21"
  },
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        "orcid": ""
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2018-06-01",
    "storage_temperature": null,
    "cell_temperature": 10.0,
    "exposure_time": 3.0,
    "number_of_frames": 300,
    "wavelength": 0.103,
    "sample_detector_distance": 1.5,
    "concentration_min": null,
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  "pddf_software": null,
  "pddf_software_version": null,
  "i0_calibration_standard": null,
  "description": "SAXS profile corresponds to a protein-DNA complex between bacterial nucleoid associated protein HUalpha and 80bp DNA. Under these conditions, the complex forms lamellar structures visible as Bragg Diffraction peaks.",
  "experiment_description": "Synchrotron SAXS data from solutions of DNA-binding protein HU-alpha bound to 80 base-pair DNA in 10 mM sodium acetate, 150 mM NaCl, pH 4.5 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS) storage ring (Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.103 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). 300 successive 3 second frames were collected at 10°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.",
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  "pddf_point_first": null,
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  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDF56_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2020-06-22T11:01:44.799841+02:00",
  "bragg_peak": []
}
查看完整 manifest.json 原文
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