SASDC72

Alcohol dehydrogenase from bifunctional alcohol/aldehyde dehydrogenase (P0A9Q8)

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Single concentration 最后更新:2021-01-04T12:08:43.215101+01:00
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1. 样品、组分与实验条件 Sample & Experiment

样品 1 · Alcohol dehydrogenase from bifunctional alcohol/aldehyde dehydrogenase (P0A9Q8)

浓度— – 10.0 缓冲液 / pH20 mM Tris 400 mM NaCl 5% v/v glycerol / 7.5
实验温度4.0 设备 / 束线Diamond Light Source / B21
波长0.1 nm曝光1.0 s × 131

分子组分

组分类型 / 物种UniProt 与构建体寡聚状态分子量
Aldehyde-alcohol dehydrogenase
查看序列
MLWHKLPKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLSIVRKGAELANSFKPDVIIALGGGSPMDAAKIMWVMYEHPETHFEELALRFMDIRKRIYKFPKMGVKAKMIAVTTTSGTGSEVTPFAVVTDDATGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAMEAYVSVLASEFSDGQALQALKLLKEYLPASYHEGSKNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLICNVIRYNANDNPTKQTAFSQYDRPQARRRYAEIADHLGLSAPGDRTAAKIEKLLAWLETLKAELGIPKSIREAGVQEADFLANVDKLSEDAFDDQCTGANPRYPLISELKQILLDTYYGRDYVEGETAAKKEAAPAKAEKKAKKSA
proteinEscherichia coli O157:H7P0A9Q8451–891dimer分子数 248.33 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
11446[3]0.004470188–0.401659 1/A含误差列缺失 04sasbdb/entries/72/sasdc72/source/SASDC72.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)16.87—Å
estimated_volumeDAMMIN178.0—ų
i0Guinier0.0617e-05—
i0P(r)0.06270.0001—
mwExperimental91.4—kDa
porod_volumePorod146.0—ų
rgGuinier3.240.06Å
rgP(r)3.550.23Å

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 400 mM NaCl 5% v/v glycerol缓冲液浓度—
pH7.5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2015-11-27储存 / 测量温度4.0 / 4.0
曝光时间1.0帧数131
波长0.1样品-探测器距离4.04
光源X-ray synchrotron探测器Pilatus 2M
机构 / 束线Diamond Light Source / B21 · Didcot, UK
q 范围0.045 – 4.017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(5 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:169 个字段值
字段路径原始值
codeSASDC72
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleHigh-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE.
project.publication.titleHigh-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE.
project.publication.author_listAzmi L, Bragginton EC, Cadby IT, Byron O, Roe AJ, Lovering AL, Gabrielsen M
project.publication.journalActa Crystallogr F Struct Biol Commun
project.publication.doi10.1107/S2053230X20010237
project.publication.pmid32880589
project.publication.published_date2020 Sep 1
project.statusreleased
project.submitted_date2017-05-11
project.released_date2017-12-12
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experiment.instrument.detector.namePilatus 2M
experiment.instrument.detector.resolutionnull
experiment.instrument.nameDiamond Light Source
experiment.instrument.cityDidcot
experiment.instrument.countryUK
experiment.instrument.beamline_nameB21
experiment.instrument.beam_geometry1 x 5 mm
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_nameAldehyde-alcohol dehydrogenase
experiment.sample.molecule[0].short_nameAdhE
experiment.sample.molecule[0].sequenceMLWHKLPKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLSIVRKGAELANSFKPDVIIALGGGSPMDAAKIMWVMYEHPETHFEELALRFMDIRKRIYKFPKMGVKAKMIAVTTTSG TGSEVTPFAVVTDDATGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAMEAYVSVLASEFSDGQALQALKLLKEYLPASYHEGSKNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLICNVIRYNANDNPTKQTAFSQYDRPQARRRYAEIADHLGLSAPGDRTAAKIEKLLAWLETLKAELGIPKSIREAGVQEADFLANVDKLSEDAFDDQCTGANPRYPLISELKQILLDTYYGRDYVEGETAAKKEAAPAKAEKKAKKSA
experiment.sample.molecule[0].organismEscherichia coli O157:H7
experiment.sample.molecule[0].uniprot_codeP0A9Q8
experiment.sample.molecule[0].uniprot_range_first451
experiment.sample.molecule[0].uniprot_range_last891
experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMAVTNVAELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMG IVEDKVIKNHFASEYIYNAYKDEKTCGVLSEDDTFGTITIAEPIGIICGIVPTTNPTSTA IFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIGWIDQPSVELSNA LMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTF DNGVICASEQSVVVVDSVYDAVRERFATHGGYLLQGKELKAVQDVILKNGALNAAIVGQP AYKIAELAGFSVPENTKILIGEVTVVDESEPFAHEKLSPTLAMYRAKDFEDAVEKAEKLV AMGGIGHTSCLYTDQDNQPARVSYFGQKMKTARILINTPASQGGIGDLYNFKLAPSLTLG CGSWGGNSISENVGPKHLINKKTVAKRAENMLWHKLPKSIYFRRGSLPIALDEVITDGHK RALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLSIVRKGAELANSFKPDVI IALGGGSPMDAAKIMWVMYEHPETHFEELALRFMDIRKRIYKFPKMGVKAKMIAVTTTSG TGSEVTPFAVVTDDATGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAME AYVSVLASEFSDGQALQALKLLKEYLPASYHEGSKNPVARERVHSAATIAGIAFANAFLG VCHSMAHKLGSQFHIPHGLANALLICNVIRYNANDNPTKQTAFSQYDRPQARRRYAEIAD HLGLSAPGDRTAAKIEKLLAWLETLKAELGIPKSIREAGVQEADFLANVDKLSEDAFDDQ CTGANPRYPLISELKQILLDTYYGRDYVEGETAAKKEAAPAKAEKKAKKSA
experiment.sample.molecule[0].mw48.33
experiment.sample.molecule[0].total_mw96.66
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
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experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
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experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameAlcohol dehydrogenase from bifunctional alcohol/aldehyde dehydrogenase (P0A9Q8)
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].addressGlasgow, Scotland, UK
experiment.contributor[0].affiliation[0].full_nameUniversity of Glasgow
experiment.contributor[0].affiliation[0].webpagehttp://www.gla.ac.uk/
experiment.contributor[0].contributor_nameLiyana
experiment.contributor[0].contributor_surnameAzmi
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2015-11-27
experiment.storage_temperature4.0
experiment.cell_temperature4.0
experiment.exposure_time1.0
experiment.number_of_frames131
experiment.wavelength0.1
experiment.sample_detector_distance4.04
experiment.concentration_minnull
experiment.concentration_max10.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.045
experiment.s_max4.017
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].softwareDAMMIF
fits[0].chi_square_value1.85
fits[0].p_value0.2137
fits[0].fit_residual_plotSASDC72_fit1_fitresiduals_img.png
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fits[0].software_versionr9217
fits[0].descriptionnull
estimated_volume_methodDAMMIN
pddf_softwareATSAS GNOM
pddf_software_versionPRIMUS 2.7.1 GNOM
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data, I(s) vs s (s = 4π sin θ/λ, where 2θ is the scattering angle and λ is the X-ray wavelength) were collected from a sample of alcohol dehydrogenase from a bifunctional alcohol/aldehyde dehydrogenase protein (P0A9Q8) using continuous-flow size-exclusion chromatography SAXS (SEC-SAXS) on the B21 beam line at the Diamond Light Source (Oxfordshire, UK). Data (131 successive 1 second frames) were collected using a Pilatus 2M detector at a sample-detector distance of 4.0 m and at a wavelength of λ = 0.1 nm. The SEC mobile phase consisted of 20 mM Tris, 400 mM NaCl, 5% v/v glycerol, pH 7.5 (4°C) with a sample injection concentration of 10 mg/ml. Data obtained from solute-free eluates and SEC-elution peak were normalized to the intensity of the transmitted beam and radially averaged. The scattering of the solvent-blank was subtracted from the SEC-peak frames using ScÅtter and then analysed using Primus to produce the data displayed in this entry.
tags[]
intensity_unitnull
experimental_mw91.4
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i00.0627
pddf_i0_error0.0001
guinier_i00.061
guinier_i0_error7e-05
pddf_rg3.55
pddf_rg_error0.23
guinier_rg3.24
guinier_rg_error0.06
pddf_dmax16.87
pddf_dmax_errornull
porod_volume146.0
porod_volume_errornull
estimated_volume178.0
estimated_volume_errornull
guinier_point_first36
guinier_point_last130
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDC72_datloglog_img.png
symmetrynull
last_modified2021-01-04T12:08:43.215101+01:00
bragg_peak[]
manifest.json:36 个字段值
字段路径原始值
codeSASDC72
statussuccess
started_at2026-08-11T16:29:37.846028+00:00
finished_at2026-08-11T16:29:46.854026+00:00
source_last_modified2021-01-04T12:08:43.215101+01:00
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查看完整 summary.json 原文
{
  "code": "SASDC72",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE.",
    "publication": {
      "title": "High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE.",
      "author_list": "Azmi L, Bragginton EC, Cadby IT, Byron O, Roe AJ, Lovering AL, Gabrielsen M",
      "journal": "Acta Crystallogr F Struct Biol Commun",
      "doi": "10.1107/S2053230X20010237",
      "pmid": "32880589",
      "published_date": "2020 Sep 1"
    },
    "status": "released",
    "submitted_date": "2017-05-11",
    "released_date": "2017-12-12"
  },
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          "long_name": "Aldehyde-alcohol dehydrogenase",
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          "organism": "Escherichia coli O157:H7",
          "uniprot_code": "P0A9Q8",
          "uniprot_range_first": 451,
          "uniprot_range_last": 891,
          "oligomerization": "dimer",
          "molecular_type": "protein",
          "uniprot_sequence": "MAVTNVAELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMG\nIVEDKVIKNHFASEYIYNAYKDEKTCGVLSEDDTFGTITIAEPIGIICGIVPTTNPTSTA\nIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIGWIDQPSVELSNA\nLMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTF\nDNGVICASEQSVVVVDSVYDAVRERFATHGGYLLQGKELKAVQDVILKNGALNAAIVGQP\nAYKIAELAGFSVPENTKILIGEVTVVDESEPFAHEKLSPTLAMYRAKDFEDAVEKAEKLV\nAMGGIGHTSCLYTDQDNQPARVSYFGQKMKTARILINTPASQGGIGDLYNFKLAPSLTLG\nCGSWGGNSISENVGPKHLINKKTVAKRAENMLWHKLPKSIYFRRGSLPIALDEVITDGHK\nRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLSIVRKGAELANSFKPDVI\nIALGGGSPMDAAKIMWVMYEHPETHFEELALRFMDIRKRIYKFPKMGVKAKMIAVTTTSG\nTGSEVTPFAVVTDDATGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAME\nAYVSVLASEFSDGQALQALKLLKEYLPASYHEGSKNPVARERVHSAATIAGIAFANAFLG\nVCHSMAHKLGSQFHIPHGLANALLICNVIRYNANDNPTKQTAFSQYDRPQARRRYAEIAD\nHLGLSAPGDRTAAKIEKLLAWLETLKAELGIPKSIREAGVQEADFLANVDKLSEDAFDDQ\nCTGANPRYPLISELKQILLDTYYGRDYVEGETAAKKEAAPAKAEKKAKKSA",
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          "molecule_source": "biological",
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      "purity_method": null,
      "name": "Alcohol dehydrogenase from bifunctional alcohol/aldehyde dehydrogenase (P0A9Q8)",
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      "absorbption": null,
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    "contributor": [
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        "affiliation": [
          {
            "short_name": null,
            "address": "Glasgow, Scotland, UK",
            "full_name": "University of Glasgow",
            "webpage": "http://www.gla.ac.uk/"
          }
        ],
        "contributor_name": "Liyana",
        "contributor_surname": "Azmi",
        "orcid": null
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    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2015-11-27",
    "storage_temperature": 4.0,
    "cell_temperature": 4.0,
    "exposure_time": 1.0,
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    "wavelength": 0.1,
    "sample_detector_distance": 4.04,
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          "model_plot": "https://www.sasbdb.org/media/pdb_file/images/SASDC72_fit1_model1_img.png",
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          "model_title": null,
          "type_of_model": "dummy",
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          "symmetry": "P2",
          "comment": "",
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      "software": "DAMMIF",
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      "fit_residual_plot": "SASDC72_fit1_fitresiduals_img.png",
      "fit_data": "https://www.sasbdb.org/media/fitting_files/SASDC72_fit1.fir",
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  "experiment_description": "Synchrotron SAXS data, I(s) vs s (s = 4π sin θ/λ, where 2θ is the scattering angle and λ is the X-ray wavelength) were collected from a sample of alcohol dehydrogenase from a bifunctional alcohol/aldehyde dehydrogenase protein (P0A9Q8) using continuous-flow size-exclusion chromatography SAXS (SEC-SAXS) on the B21 beam line at the Diamond Light Source (Oxfordshire, UK). Data (131 successive 1 second frames) were collected using a Pilatus 2M detector at a sample-detector distance of 4.0 m and at a wavelength of λ = 0.1 nm. The SEC mobile phase consisted of 20 mM Tris, 400 mM NaCl, 5% v/v glycerol, pH 7.5 (4°C) with a sample injection concentration of 10 mg/ml. Data obtained from solute-free eluates and SEC-elution peak were normalized to the intensity of the transmitted beam and radially averaged. The scattering of the solvent-blank was subtracted from the SEC-peak frames using ScÅtter and then analysed using Primus to produce the data displayed in this entry.",
  "tags": [],
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  "intensities_log_log_plot": "SASDC72_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2021-01-04T12:08:43.215101+01:00",
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}
查看完整 manifest.json 原文
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