SASDDB4

p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 4 mg/ml of S172A C1 in 1 mM 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): 4 mg/ml of S172A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

Concentration— – 4.0 Buffer / pH50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 5% glycerol, 1 mM HPA / 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 S172A mutant
View sequence
MNQLNTAIVEKEVIDPMAFRRALGNFATGVTIMTAQTSSGERVGVTANSFNSVSLDPALVLWSIDKKSSSYRIFEEATHFGVNILSAAQIELSNRFARRSEDKFANIEFDLGVGNIPLFKNCSAAFECERYNIVEGGDHWIIIGRVVKFHDHGRSPLLYHQGAYSAVLPHPALNMKSETAEGVFPGRLYDNMYYLLTQAVRAYQNDYQPKQLASGFRTSEARLLLVLESKTASSKCDLQREVAMPIREIEEATKILSEKGLLIDNGQHYELTEQGNACAHMLYKIAESHQEEVFAKYTVDERKLFKNMLKDLIGI
proteinAcinetobacter baumannii——–—dimerMolecule count 235.396 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1913[3]0.0299702264–0.278066881 1/AHas uncertainty columnMissing 019sasbdb/entries/b4/sasddb4/source/SASDDB4.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)8.63—Å
i0Guinier176.430.85arbitrary
i0P(r)185.5—arbitrary
mwExperimental72.0—kDa
mwPorod61.0—kDa
porod_volumePorod98.0—ų
rgGuinier2.7730.015Å
rgP(r)2.92—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, 5% glycerol, 1 mM HPABuffer 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

Downloadable Files

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full_entry_zip:source record and ZIP contents (2 items)
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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
codeSASDDB4
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.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
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experiment.instrument.line_collimation_slitlengthnull
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experiment.instrument.xray_energynull
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experiment.sample.molecule[0].long_namep-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A mutant
experiment.sample.molecule[0].short_nameS172A C1 reductase
experiment.sample.molecule[0].sequenceMNQLNTAIVE KEVIDPMAFR RALGNFATGV TIMTAQTSSG ERVGVTANSF NSVSLDPALV LWSIDKKSSS YRIFEEATHF GVNILSAAQI ELSNRFARRS EDKFANIEFD LGVGNIPLFK NCSAAFECER YNIVEGGDHW IIIGRVVKFH DHGRSPLLYH QGAYSAVLPH PALNMKSETA 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].mw35.396
experiment.sample.molecule[0].total_mw70.792
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, 5% glycerol, 1 mM HPA
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): 4 mg/ml of S172A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)
experiment.sample.ext_coefficientnull
experiment.sample.contrastnull
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experiment.sample.dry_volnull
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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
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experiment.concentration_unitnull
experiment.date2017-03-07
experiment.storage_temperature4.0
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experiment.exposure_time600.0
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experiment_descriptionnull
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guinier_point_last62
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intensities_log_log_plotSASDDB4_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDDB4
statussuccess
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finished_at2026-08-11T14:18:27.236324+00:00
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View the complete summary.json source
{
  "code": "SASDDB4",
  "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.",
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      "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",
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View the complete manifest.json source
{
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