SASDD28

p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of E251A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Single concentration 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 · p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of E251A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

浓度— – 2.0 缓冲液 / pH50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, 10 % glycerol / 7.0
实验温度16.0 设备 / 束线Synchrotron Light Research Institute (SLRI) / BL1.3W
波长0.13776 nm曝光600.0 s × 1

分子组分

组分类型 / 物种UniProt 与构建体寡聚状态分子量
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant
查看序列
>GI|45685345|GB|AAS75430.1|P-HYDROXYPHENYLACETATEHYDROXYLASEC1:REDUCTASECOMPONENT[ACINETOBACTERBAUMANNII]MNQLNTAIVEKEVIDPMAFRRALGNFATGVTIMTAQTSSGERVGVTANSFNSVSLDPALVLWSIDKKSSSYRIFEEATHFGVNILSAAQIELSNRFARRSEDKFANIEFDLGVGNIPLFKNCSAAFECERYNIVEGGDHWIIIGRVVKFHDHGRSPLLYHQGAYSAVLPHPSLNMKSETAEGVFPGRLYDNMYYLLTQAVRAYQNDYQPKQLASGFRTSEARLLLVLESKTASSKCDLQREVAMPIREIEAATKILSEKGLLIDNGQHYELTEQGNACAHMLYKIAESHQEEVFAKYTVDERKLFKNMLKDLIGI
proteinAcinetobacter baumanniiQ6Q271—–—dimer分子数 235.354 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
1922[3]0.0299079354–0.27992731 1/A含误差列缺失 02sasbdb/entries/28/sasdd28/source/SASDD28.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)8.37—Å
i0Guinier53.690.47arbitrary
i0P(r)54.57—arbitrary
mwExperimental56.0—kDa
porod_volumePorod89.0—ų
rgGuinier2.5740.086Å
rgP(r)2.6—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50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, 10 % glycerol缓冲液浓度—
pH7.0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2018-04-25储存 / 测量温度4.0 / 16.0
曝光时间600.0帧数1
波长0.13776样品-探测器距离1.332
光源X-ray synchrotron探测器Rayonix SX165
机构 / 束线Synchrotron Light Research Institute (SLRI) / BL1.3W · Nakhon Ratchasima, Thailand
q 范围0.299 – 2.799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(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:134 个字段值
字段路径原始值
codeSASDD28
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleCrystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands.
project.publication.titleCrystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands.
project.publication.author_listYuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D
project.publication.journalArch Biochem Biophys
project.publication.doi10.1016/j.abb.2018.06.010
project.publication.pmid29940152
project.publication.published_date2018 Sep 1
project.statusreleased
project.submitted_date2018-06-05
project.released_date2018-06-29
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experiment.instrument.detector.nameRayonix SX165
experiment.instrument.detector.resolution15.0
experiment.instrument.nameSynchrotron Light Research Institute (SLRI)
experiment.instrument.cityNakhon Ratchasima
experiment.instrument.countryThailand
experiment.instrument.beamline_nameBL1.3W
experiment.instrument.beam_geometrynull
experiment.instrument.type_of_sourceX-ray synchrotron
experiment.instrument.point_sourcenull
experiment.instrument.line_collimationnull
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experiment.instrument.xray_energynull
experiment.instrument.beam_profile_ahnull
experiment.instrument.beam_profile_alnull
experiment.sample.molecule[0].long_namep-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant
experiment.sample.molecule[0].short_nameE251A C1
experiment.sample.molecule[0].sequence>gi|45685345|gb|AAS75430.1| p-hydroxyphenylacetate hydroxylase C1:reductase component [Acinetobacter baumannii] MNQLNTAIVEKEVIDPMAFRRALGNFATGVTIMTAQTSSGERVGVTANSFNSVSLDPALVLWSIDKKSSS YRIFEEATHFGVNILSAAQIELSNRFARRSEDKFANIEFDLGVGNIPLFKNCSAAFECERYNIVEGGDHW IIIGRVVKFHDHGRSPLLYHQGAYSAVLPHPSLNMKSETAEGVFPGRLYDNMYYLLTQAVRAYQNDYQPK QLASGFRTSEARLLLVLESKTASSKCDLQREVAMPIREIEAATKILSEKGLLIDNGQHYELTEQGNACAH MLYKIAESHQEEVFAKYTVDERKLFKNMLKDLIGI
experiment.sample.molecule[0].organismAcinetobacter baumannii
experiment.sample.molecule[0].uniprot_codeQ6Q271
experiment.sample.molecule[0].uniprot_range_firstnull
experiment.sample.molecule[0].uniprot_range_lastnull
experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
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experiment.sample.molecule[0].mw35.354
experiment.sample.molecule[0].total_mw70.708
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.buffer.name50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, 10 % 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.ph7.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.namep-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of E251A C1 in the absence of p-hydroxyphenylacetic acid (HPA)
experiment.sample.ext_coefficientnull
experiment.sample.contrastnull
experiment.sample.specific_volnull
experiment.sample.dry_volnull
experiment.sample.absorbptionnull
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experiment.sample.mixturenull
experiment.contributor[0].affiliation[0].short_namenull
experiment.contributor[0].affiliation[0].addressThailand
experiment.contributor[0].affiliation[0].full_nameMahidol University
experiment.contributor[0].affiliation[0].webpagehttps://mahidol.ac.th/
experiment.contributor[0].contributor_nameAnan
experiment.contributor[0].contributor_surnameYuenyao
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2018-04-25
experiment.storage_temperature4.0
experiment.cell_temperature16.0
experiment.exposure_time600.0
experiment.number_of_frames1
experiment.wavelength0.13776
experiment.sample_detector_distance1.332
experiment.concentration_minnull
experiment.concentration_max2.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.299
experiment.s_max2.799
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionnull
tags[]
intensity_unitarbitrary
experimental_mw56.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i054.57
pddf_i0_errornull
guinier_i053.69
guinier_i0_error0.47
pddf_rg2.6
pddf_rg_errornull
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guinier_rg_error0.086
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pddf_dmax_errornull
porod_volume89.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first1
guinier_point_last76
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDD28_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
codeSASDD28
statussuccess
started_at2026-08-11T15:43:54.713519+00:00
finished_at2026-08-11T15:44:04.445397+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": "SASDD28",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands.",
    "publication": {
      "title": "Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands.",
      "author_list": "Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D",
      "journal": "Arch Biochem Biophys",
      "doi": "10.1016/j.abb.2018.06.010",
      "pmid": "29940152",
      "published_date": "2018 Sep 1"
    },
    "status": "released",
    "submitted_date": "2018-06-05",
    "released_date": "2018-06-29"
  },
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        }
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}
查看完整 manifest.json 原文
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