SASDCH2

Aldehyde dehydrogenase 7A1

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 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. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Aldehyde dehydrogenase 7A1

Concentration— – — Buffer / pH50 mM Tris, 5% glycerol, 0.5 mM tris(3-hydroxypropyl)phosphine, 50 mM NaCl / 7.8
Experimental temperature— Facility / beamlineAdvanced Light Source (ALS) / 12.3.1 (SIBYLS)
Wavelength— nmExposure— s × —

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Aldehyde dehydrogenase 7A1 (Alpha-aminoadipic semialdehyde dehydrogenase)
View sequence
GHMSTLLINQPQYAWLKELGLREENEGVYNGSWGGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYSKDLPLAQGIKFQ
proteinHomo sapiensP49419—–—tetramerMolecule count 455.56 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1509[3]0.009426–0.318927 1/AHas uncertainty columnMissing 00sasbdb/entries/h2/sasdch2/source/SASDCH2.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
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

These values are reported by SASBDB; SAXSdb did not recalculate them from the experimental curve.

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3. Source Fits and Models Source Fits & Models

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4. Source File Index Source Files

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5. Experiment Description and Publication Experiment & Publication

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6. Complete Source Record Complete Source Record

The following content comes directly from the SASBDB entry. Missing values are shown as “—”; SAXSdb does not infer undeclared units.

Open the original SASBDB entry

Buffer and Sample Properties

Buffer name50 mM Tris, 5% glycerol, 0.5 mM tris(3-hydroxypropyl)phosphine, 50 mM NaClBuffer concentration—
pH7.8Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2014-03-09Storage / measurement temperature— / —
Exposure time—Frames—
Wavelength—Sample-to-detector distance—
SourceX-ray synchrotronDetectorMAR 165 CCD
Facility / beamlineAdvanced Light Source (ALS) / 12.3.1 (SIBYLS) · Berkeley, CA, USA
q range0.094 – 3.189Sample volume / flow rate— / —

Original SASBDB Plots

Experimental I(q)
Experimental I(q)
Experimental I(q), log-log
Experimental I(q), log-log
Guinier plot
Guinier plot
Kratky plot
Kratky plot
P(r) plot
P(r) plot

Downloadable Files

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All source fields (unfiltered)

Every source field is expanded here, including empty values, list members and fields already shown above.

summary.json:159 field values
Field pathRaw value
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
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experiment.instrument.sample_path_lengthnull
experiment.instrument.line_collimation_slitlengthnull
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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
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experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
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experiment.sample.purity_methodnull
experiment.sample.nameAldehyde dehydrogenase 7A1
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experiment.sample.contrastnull
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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
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fits[0].models[0].bead_radius1.9
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fits[0].models[0].user166
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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
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guinier_i0_mwnull
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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 field values
Field pathRaw value
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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View the complete summary.json source
{
  "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"
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    "status": "released",
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          "long_name": "Aldehyde dehydrogenase 7A1 (Alpha-aminoadipic semialdehyde dehydrogenase)",
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          "sequence": "GHMSTLLINQPQYAWLKELGLREENEGVYNGSWGGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIP\r\nAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVG\r\nLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDER\r\nVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEV\r\nVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHT\r\nETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGR\r\nESGSDAWKQYMRRSTCTINYSKDLPLAQGIKFQ",
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          "uniprot_range_last": null,
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      "name": "Aldehyde dehydrogenase 7A1",
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        "affiliation": [
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            "short_name": "Mizzou",
            "address": "Columbia, MO, USA",
            "full_name": "University of Missouri-Columbia",
            "webpage": "http://missouri.edu/"
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  "last_modified": "2026-05-18T10:07:55.214115+02:00",
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View the complete manifest.json source
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