SASDDD4

p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of N174A 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 N174A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

Concentration— – 2.0 Buffer / pH50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, and 5% 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 N174A mutant
View sequence
MNQLNTAIVEKEVIDPMAFRRALGNFATGVTIMTAQTSSGERVGVTANSFNSVSLDPALVLWSIDKKSSSYRIFEEATHFGVNILSAAQIELSNRFARRSEDKFANIEFDLGVGNIPLFKNCSAAFECERYNIVEGGDHWIIIGRVVKFHDHGRSPLLYHQGAYSAVLPHPSLAMKSETAEGVFPGRLYDNMYYLLTQAVRAYQNDYQPKQLASGFRTSEARLLLVLESKTASSKCDLQREVAMPIREIEEATKILSEKGLLIDNGQHYELTEQGNACAHMLYKIAESHQEEVFAKYTVDERKLFKNMLKDLIGI
proteinAcinetobacter baumannii——–—dimerMolecule count 235.369 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1913[3]0.0299702264–0.278066881 1/AHas uncertainty columnMissing 011sasbdb/entries/d4/sasddd4/source/SASDDD4.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)7.0—Å
i0Guinier65.470.6arbitrary
i0P(r)69.87—arbitrary
mwExperimental71.0—kDa
mwPorod76.0—kDa
porod_volumePorod93.0—ų
rgGuinier2.3980.023Å
rgP(r)2.5150.005Å

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, and 5% 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 date2017-03-07Storage / measurement temperature4.0 / 16.0
Exposure time600.0Frames1
Wavelength0.13776Sample-to-detector distance1.3323
SourceX-ray synchrotronDetectorRayonix SX165
Facility / beamlineSynchrotron Light Research Institute (SLRI) / BL1.3W · Nakhon Ratchasima, Thailand
q range0.3 – 2.781Sample 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

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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
codeSASDDD4
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_date2018-02-28
project.released_date2018-06-27
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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 N174A mutant
experiment.sample.molecule[0].short_nameN174A C1 reductase
experiment.sample.molecule[0].sequenceMNQLNTAIVE KEVIDPMAFR RALGNFATGV TIMTAQTSSG ERVGVTANSF NSVSLDPALV LWSIDKKSSS YRIFEEATHF GVNILSAAQI ELSNRFARRS EDKFANIEFD LGVGNIPLFK NCSAAFECER YNIVEGGDHW IIIGRVVKFH DHGRSPLLYH QGAYSAVLPH PSLAMKSETA EGVFPGRLYD NMYYLLTQAV RAYQNDYQPK QLASGFRTSE ARLLLVLESK TASSKCDLQR EVAMPIREIE EATKILSEKG LLIDNGQHYE LTEQGNACAH MLYKIAESHQ EEVFAKYTVD ERKLFKNMLK DLIGI
experiment.sample.molecule[0].organismAcinetobacter baumannii
experiment.sample.molecule[0].uniprot_codenull
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_sequencenull
experiment.sample.molecule[0].mw35.369
experiment.sample.molecule[0].total_mw70.738
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, and 5% glycerol
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
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experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.0
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experiment.sample.purity_methodnull
experiment.sample.namep-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of N174A C1 in the absence of p-hydroxyphenylacetic acid (HPA)
experiment.sample.ext_coefficientnull
experiment.sample.contrastnull
experiment.sample.specific_volnull
experiment.sample.dry_volnull
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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.date2017-03-07
experiment.storage_temperature4.0
experiment.cell_temperature16.0
experiment.exposure_time600.0
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experiment.s_min0.3
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intensities_log_log_plotSASDDD4_1_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDDD4
statussuccess
started_at2026-08-11T14:20:28.133837+00:00
finished_at2026-08-11T14:20:36.585077+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDDD4",
  "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"
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View the complete manifest.json source
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