SASDCH2

Aldehyde dehydrogenase 7A1

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Single concentration 最后更新:2026-05-18T10:07:55.214115+02:00

The FoXS fits have χ values of 1.5 for the tetramer, 12.4 for the dimer, and 1.2 for the 96%/4% tetramer/dimer ensemble.

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1. 样品、组分与实验条件 Sample & Experiment

样品 1 · Aldehyde dehydrogenase 7A1

浓度— – — 缓冲液 / pH50 mM Tris, 5% glycerol, 0.5 mM tris(3-hydroxypropyl)phosphine, 50 mM NaCl / 7.8
实验温度— 设备 / 束线Advanced Light Source (ALS) / 12.3.1 (SIBYLS)
波长— nm曝光— s × —

分子组分

组分类型 / 物种UniProt 与构建体寡聚状态分子量
Aldehyde dehydrogenase 7A1 (Alpha-aminoadipic semialdehyde dehydrogenase)
查看序列
GHMSTLLINQPQYAWLKELGLREENEGVYNGSWGGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYSKDLPLAQGIKFQ
proteinHomo sapiensP49419—–—tetramer分子数 455.56 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
1509[3]0.009426–0.318927 1/A含误差列缺失 00sasbdb/entries/h2/sasdch2/source/SASDCH2.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)11.50.5Å
i0Guinier853.010.0—
i0P(r)848.04.0—
mwExperimental222.2—kDa
porod_volumePorod270.0—ų
rgGuinier3.770.05Å
rgP(r)3.710.01Å

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50 mM Tris, 5% glycerol, 0.5 mM tris(3-hydroxypropyl)phosphine, 50 mM NaCl缓冲液浓度—
pH7.8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2014-03-09储存 / 测量温度— / —
曝光时间—帧数—
波长—样品-探测器距离—
光源X-ray synchrotron探测器MAR 165 CCD
机构 / 束线Advanced Light Source (ALS) / 12.3.1 (SIBYLS) · Berkeley, CA, USA
q 范围0.094 – 3.189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/h2/sasdch2/source/SASDCH2.zipdownloaded330815808b543c32fff8da7a84d9c38731898eb09b14eace927eac3f28576195f8254f下载查看原文件源站
pddfsasbdb/entries/h2/sasdch2/source/SASDCH2.outdownloaded40331965b3b7c6068f266ef2568664e73e3618421c40e12889c533778285e3ab8d355下载查看原文件源站
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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(4 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:159 个字段值
字段路径原始值
codeSASDCH2
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleStructural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1.
project.publication.titleStructural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1.
project.publication.author_listLuo M, Tanner JJ
project.publication.journalBiochemistry
project.publication.doi10.1021/acs.biochem.5b00754
project.publication.pmid26260980
project.publication.published_date2015 Sep 8
project.statusreleased
project.submitted_date2016-10-05
project.released_date2017-04-03
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experiment.instrument.detector.typenull
experiment.instrument.detector.nameMAR 165 CCD
experiment.instrument.detector.resolutionnull
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_nameAldehyde dehydrogenase 7A1 (Alpha-aminoadipic semialdehyde dehydrogenase)
experiment.sample.molecule[0].short_nameALDH7A1
experiment.sample.molecule[0].sequenceGHMSTLLINQPQYAWLKELGLREENEGVYNGSWGGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIP APKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVG LVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDER VNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEV VNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHT ETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGR ESGSDAWKQYMRRSTCTINYSKDLPLAQGIKFQ
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeP49419
experiment.sample.molecule[0].uniprot_range_firstnull
experiment.sample.molecule[0].uniprot_range_lastnull
experiment.sample.molecule[0].oligomerizationtetramer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMWRLPRALCVHAAKTSKLSGPWSRPAAFMSTLLINQPQYAWLKELGLREENEGVYNGSWG GRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDA LREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIE QWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLED NKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGN NAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVG NPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHD ASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGI VNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYSKDLPLAQGIKFQ
experiment.sample.molecule[0].mw55.56
experiment.sample.molecule[0].total_mw222.24
experiment.sample.molecule[0].number_molecules4
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 Tris, 5% glycerol, 0.5 mM tris(3-hydroxypropyl)phosphine, 50 mM NaCl
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
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experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.8
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameAldehyde dehydrogenase 7A1
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_nameMizzou
experiment.contributor[0].affiliation[0].addressColumbia, MO, USA
experiment.contributor[0].affiliation[0].full_nameUniversity of Missouri-Columbia
experiment.contributor[0].affiliation[0].webpagehttp://missouri.edu/
experiment.contributor[0].contributor_nameJohn
experiment.contributor[0].contributor_surnameTanner
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2014-03-09
experiment.storage_temperaturenull
experiment.cell_temperaturenull
experiment.exposure_timenull
experiment.number_of_framesnull
experiment.wavelengthnull
experiment.sample_detector_distancenull
experiment.concentration_minnull
experiment.concentration_maxnull
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.094
experiment.s_max3.189
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].softwareFoXS
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fits[0].models[0].bead_radius1.9
fits[0].models[0].lognull
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fits[0].models[0].commentchains A, B, C, and D of PDB 4ZUK
fits[0].models[0].user166
fits[0].fit_unit1/A
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fits[0].softwarenull
fits[0].chi_square_value1.63
fits[0].p_value0.0
fits[0].fit_residual_plotSASDCH2_fit1_fitresiduals_img.png
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fits[0].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionGNOM
i0_calibration_standardnull
descriptionThe FoXS fits have χ values of 1.5 for the tetramer, 12.4 for the dimer, and 1.2 for the 96%/4% tetramer/dimer ensemble.
experiment_descriptionSynchrotron SAXS data from solutions of Aldehyde dehydrogenase 7A1 in 50 mM Tris, 5% glycerol, 0.5 mM tris(3-hydroxypropyl)phosphine, 50 mM NaCl, pH 7.8 were collected on the 12.3.1 (SIBYLS) camera on the storage ring Advanced Light Source (ALS) (Berkeley, CA, USA) via the mail-in program. Prior to data collection, an ALDH7A1 sample was passed through a Superdex 200 size exclusion column. Scattering intensities were measured at three nominal protein concentrations using exposure times of 0.5, 1.0, 3.0, and 6.0 s. Scattering curves collected from the protein samples were corrected for background scattering using intensity data collected from the Superdex 200 column effluent. Composite scattering curves for each protein concentration were generated with PRIMUS by scaling and merging the background-corrected high-s region from the 3 s exposure with the low-s region from the 0.5 or 1.0 s exposure.
tags[]
intensity_unitnull
experimental_mw222.2
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i0848.0
pddf_i0_error4.0
guinier_i0853.0
guinier_i0_error10.0
pddf_rg3.71
pddf_rg_error0.01
guinier_rg3.77
guinier_rg_error0.05
pddf_dmax11.5
pddf_dmax_error0.5
porod_volume270.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first1
guinier_point_last40
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDCH2_datloglog_img.png
symmetrynull
last_modified2026-05-18T10:07:55.214115+02:00
bragg_peak[]
manifest.json:36 个字段值
字段路径原始值
codeSASDCH2
statussuccess
started_at2026-08-11T13:38:43.422221+00:00
finished_at2026-08-11T13:38:53.376323+00:00
source_last_modified2026-05-18T10:07:55.214115+02:00
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查看完整 summary.json 原文
{
  "code": "SASDCH2",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1.",
    "publication": {
      "title": "Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1.",
      "author_list": "Luo M, Tanner JJ",
      "journal": "Biochemistry",
      "doi": "10.1021/acs.biochem.5b00754",
      "pmid": "26260980",
      "published_date": "2015 Sep 8"
    },
    "status": "released",
    "submitted_date": "2016-10-05",
    "released_date": "2017-04-03"
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          "long_name": "Aldehyde dehydrogenase 7A1 (Alpha-aminoadipic semialdehyde dehydrogenase)",
          "short_name": "ALDH7A1",
          "sequence": "GHMSTLLINQPQYAWLKELGLREENEGVYNGSWGGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIP\r\nAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVG\r\nLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDER\r\nVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEV\r\nVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHT\r\nETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGR\r\nESGSDAWKQYMRRSTCTINYSKDLPLAQGIKFQ",
          "organism": "Homo sapiens",
          "uniprot_code": "P49419",
          "uniprot_range_first": null,
          "uniprot_range_last": null,
          "oligomerization": "tetramer",
          "molecular_type": "protein",
          "uniprot_sequence": "MWRLPRALCVHAAKTSKLSGPWSRPAAFMSTLLINQPQYAWLKELGLREENEGVYNGSWG\nGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDA\nLREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIE\nQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLED\nNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGN\nNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVG\nNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHD\nASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGI\nVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYSKDLPLAQGIKFQ",
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          "number_molecules": 4,
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          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        }
      ],
      "buffer": {
        "name": "50 mM Tris, 5% glycerol, 0.5 mM tris(3-hydroxypropyl)phosphine, 50 mM NaCl",
        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 7.8,
        "deuteration": null
      },
      "purity_method": null,
      "name": "Aldehyde dehydrogenase 7A1",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": "Mizzou",
            "address": "Columbia, MO, USA",
            "full_name": "University of Missouri-Columbia",
            "webpage": "http://missouri.edu/"
          }
        ],
        "contributor_name": "John",
        "contributor_surname": "Tanner",
        "orcid": null
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2014-03-09",
    "storage_temperature": null,
    "cell_temperature": null,
    "exposure_time": null,
    "number_of_frames": null,
    "wavelength": null,
    "sample_detector_distance": null,
    "concentration_min": null,
    "concentration_max": null,
    "sample_volume": null,
    "flow_rate": null,
    "s_min": 0.094,
    "s_max": 3.189,
    "total_exposure_time": null,
    "seccolumn": null
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              "ext_code": "4ZUK",
              "ext_type": "pdb",
              "difference_with_model": "derived"
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          "type_of_model": "atomic",
          "software_version": "",
          "model_data": "https://www.sasbdb.org/media/pdb_file/SASDCH2_fit1_model1.pdb",
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          "bead_radius": 1.9,
          "log": null,
          "symmetry": "",
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          "user": 166
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      "fit_unit": "1/A",
      "fit_plot": "https://www.sasbdb.org/media/fitting_files/scattering_plots/SASDCH2_fit1_fixed_fit_img.png",
      "software": null,
      "chi_square_value": 1.63,
      "p_value": 0.0,
      "fit_residual_plot": "SASDCH2_fit1_fitresiduals_img.png",
      "fit_data": "https://www.sasbdb.org/media/fitting_files/SASDCH2_fit1.fit",
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  "description": "The FoXS fits have χ values of 1.5 for the tetramer, 12.4 for the dimer, and 1.2 for the 96%/4% tetramer/dimer ensemble.",
  "experiment_description": "Synchrotron SAXS data from solutions of Aldehyde dehydrogenase 7A1 in 50 mM Tris, 5% glycerol, 0.5 mM tris(3-hydroxypropyl)phosphine, 50 mM NaCl, pH 7.8 were collected on the 12.3.1 (SIBYLS) camera on the storage ring Advanced Light Source (ALS) (Berkeley, CA, USA) via the mail-in program. Prior to data collection, an ALDH7A1 sample was passed through a Superdex 200 size exclusion column. Scattering intensities were measured at three nominal protein concentrations using exposure times of 0.5, 1.0, 3.0, and 6.0 s. Scattering curves collected from the protein samples were corrected for background scattering using intensity data collected from the Superdex 200 column effluent. Composite scattering curves for each protein concentration were generated with PRIMUS by scaling and merging the background-corrected high-s region from the 3 s exposure with the low-s region from the 0.5 or 1.0 s exposure.",
  "tags": [],
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  "guinier_point_first": 1,
  "guinier_point_last": 40,
  "pddf_point_first": null,
  "pddf_point_last": null,
  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDCH2_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2026-05-18T10:07:55.214115+02:00",
  "bragg_peak": []
}
查看完整 manifest.json 原文
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