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SASDD28

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

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2019-12-06T13:07:15.624532+01:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of E251A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

Concentration— – 2.0 Buffer / pH50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, 10 % glycerol / 7.0
Experimental temperature16.0 Facility / beamlineSynchrotron Light Research Institute (SLRI) / BL1.3W
Wavelength0.13776 nmExposure600.0 s × 1

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant
View sequence
>GI|45685345|GB|AAS75430.1|P-HYDROXYPHENYLACETATEHYDROXYLASEC1:REDUCTASECOMPONENT[ACINETOBACTERBAUMANNII]MNQLNTAIVEKEVIDPMAFRRALGNFATGVTIMTAQTSSGERVGVTANSFNSVSLDPALVLWSIDKKSSSYRIFEEATHFGVNILSAAQIELSNRFARRSEDKFANIEFDLGVGNIPLFKNCSAAFECERYNIVEGGDHWIIIGRVVKFHDHGRSPLLYHQGAYSAVLPHPSLNMKSETAEGVFPGRLYDNMYYLLTQAVRAYQNDYQPKQLASGFRTSEARLLLVLESKTASSKCDLQREVAMPIREIEAATKILSEKGLLIDNGQHYELTEQGNACAHMLYKIAESHQEEVFAKYTVDERKLFKNMLKDLIGI
proteinAcinetobacter baumanniiQ6Q271—–—dimerMolecule count 235.354 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1922[3]0.0299079354–0.27992731 1/AHas uncertainty columnMissing 02sasbdb/entries/28/sasdd28/source/SASDD28.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
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

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

This entry has no source fit record.

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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 MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, 10 % glycerolBuffer concentration—
pH7.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2018-04-25Storage / measurement temperature4.0 / 16.0
Exposure time600.0Frames1
Wavelength0.13776Sample-to-detector distance1.332
SourceX-ray synchrotronDetectorRayonix SX165
Facility / beamlineSynchrotron Light Research Institute (SLRI) / BL1.3W · Nakhon Ratchasima, Thailand
q range0.299 – 2.799Sample 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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full_entry_zip：source record and ZIP contents (2 items)
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pddf：source record
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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：134 field values
Field pathRaw value
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
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDD28.out
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intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDD28_kratky_img.png
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experiment.instrument.detector.typeCCD
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
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_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
experiment.sample.molecule[0].uniprot_sequenceMNQLNTAIVEKEVIDPMAFRRALGNFATGVTIMTAQTSSGERVGVTANSFNSVSLDPALV LWSIDKKSSSYRIFEEATHFGVNILSAAQIELSNRFARRSEDKFANIEFDLGVGNIPLFK NCSAAFECERYNIVEGGDHWIIIGRVVKFHDHGRSPLLYHQGAYSAVLPHPSLNMKSETA EGVFPGRLYDNMYYLLTQAVRAYQNDYQPKQLASGFRTSEARLLLVLESKTASSKCDLQR EVAMPIREIEEATKILSEKGLLIDNGQHYELTEQGNACAHMLYKIAESHQEEVFAKYTVD ERKLFKNMLKDLIGI
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
experiment.sample.deuterationnull
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
guinier_rg2.574
guinier_rg_error0.086
pddf_dmax8.37
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 field values
Field pathRaw value
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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View the complete summary.json source
{
  "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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      "beamline_name": "BL1.3W",
      "beam_geometry": null,
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        {
          "long_name": "p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant",
          "short_name": "E251A C1",
          "sequence": ">gi|45685345|gb|AAS75430.1| p-hydroxyphenylacetate hydroxylase C1:reductase component [Acinetobacter baumannii]\r\nMNQLNTAIVEKEVIDPMAFRRALGNFATGVTIMTAQTSSGERVGVTANSFNSVSLDPALVLWSIDKKSSS\r\nYRIFEEATHFGVNILSAAQIELSNRFARRSEDKFANIEFDLGVGNIPLFKNCSAAFECERYNIVEGGDHW\r\nIIIGRVVKFHDHGRSPLLYHQGAYSAVLPHPSLNMKSETAEGVFPGRLYDNMYYLLTQAVRAYQNDYQPK\r\nQLASGFRTSEARLLLVLESKTASSKCDLQREVAMPIREIEAATKILSEKGLLIDNGQHYELTEQGNACAH\r\nMLYKIAESHQEEVFAKYTVDERKLFKNMLKDLIGI",
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      "ext_coefficient": null,
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View the complete manifest.json source
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