SASDDJ7

Citrate-binding PAS domain from the sensor histidine kinase, CitA, fused to lipase EstA

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2019-12-06T13:07:15.624532+01:00

The protein is a fusion of: i) CitAP - the PAS domain from Sensor histidine kinase, CitA, from Klebsiella pneumoniae; UniProt: P52687 (Amino acid range 45-177); ii) BsLA - the Lipase EstA from Bacillus subtilis 168; UniProt: I6V559 (Amino acid range 32-212) and; iii) A linker connecting CitAP with EstA - derived from the blue light photoreceptor, YtvA, from Bacillus subtilis 168; UniProt: O34627 (Amino acid range 132-147).

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Citrate-binding PAS domain from the sensor histidine kinase, CitA, fused to lipase EstA

Concentration— – 4.98 Buffer / pH10 mM glycine buffer, 10 mM NaCl / 10.0
Experimental temperature20.0 Facility / beamlineESRF / BM29
Wavelength0.09919 nmExposure1.0 s × 10

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
citrate-binding CitAP domain fused to lipase A of Bacillus subtilis BsLA
View sequence
>CITAP-BSLAMGSSHHHHHHSSGLVPRGSHMDITEERLHYQVGQRALIQAMQISAMPELVEAVQKRDLARIKALIDPMRSFSDATYITVGDASGQRLYHVNPDEIGKSMEGGDSDEALINAKSYVSVRKGSLGSSLRGKSPIQDATGKVIGIVSVGYTIEQLENYEKLLEDSLTEITALSIEGREAEHNPVVMVHGIGGASFNFAGIKSYLVSQGWSRDKLYAVDFWDKTGTNYNNGPVLSRFVQKVLDETGAKKVDIVAHSMGGANTLYYIKNLDGGNKVANVVTLGGANRLTTGKALPGTDPNQKILYTSIYSSADMIVMNYLSRLDGARNVQIHGVGHIGLLYSSQVNSLIKEGLNGGGQNTN
protein———–—dimerMolecule count 238.495 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11036[3]0.03605559–5.011726 1/nmHas uncertainty columnMissing 03sasbdb/entries/j7/sasddj7/source/SASDDJ7.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)11.81—nm
i0Guinier84.420.068arbitrary
i0P(r)85.43—arbitrary
mwExperimental84.42—kDa
mwGuinier I(0)84.420.068kDa
rgGuinier3.320.06nm
rgP(r)3.423—nm

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 name10 mM glycine buffer, 10 mM NaClBuffer concentration—
pH10.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2014-02-06Storage / measurement temperature20.0 / 20.0
Exposure time1.0Frames10
Wavelength0.09919Sample-to-detector distance2.849
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineESRF / BM29 · Grenoble, France
q range0.036 – 5.012Sample 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:169 field values
Field pathRaw value
codeSASDDJ7
statusPublished
type_of_curveSingle concentration
angular_unit1/nm
project.titleA combination of mutational and computational scanning guides the design of an artificial ligand-binding controlled lipase.
project.publication.titleA combination of mutational and computational scanning guides the design of an artificial ligand-binding controlled lipase.
project.publication.author_listKaschner M, Schillinger O, Fettweiss T, Nutschel C, Krause F, Fulton A, Strodel B, Stadler A, Jaeger KE, Krauss U
project.publication.journalSci Rep
project.publication.doi10.1038/srep42592
project.publication.pmid28218303
project.publication.published_date2017 Feb 20
project.statusreleased
project.submitted_date2018-05-17
project.released_date2018-06-05
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experiment.instrument.detector.namePilatus 1M
experiment.instrument.detector.resolution172.0
experiment.instrument.nameESRF
experiment.instrument.cityGrenoble
experiment.instrument.countryFrance
experiment.instrument.beamline_nameBM29
experiment.instrument.beam_geometry
experiment.instrument.type_of_sourceX-ray synchrotron
experiment.instrument.point_sourcenull
experiment.instrument.line_collimationnull
experiment.instrument.sample_path_lengthnull
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experiment.sample.molecule[0].long_namecitrate-binding CitAP domain fused to lipase A of Bacillus subtilis BsLA
experiment.sample.molecule[0].short_nameCitAP-BsLA
experiment.sample.molecule[0].sequence>CitAP-BsLA MGSSHHHHHHSSGLVPRGSHMDITEERLHYQVGQRALIQAMQISAMPELVEAVQKRDLARIKALIDPMRSFSDATYITVG DASGQRLYHVNPDEIGKSMEGGDSDEALINAKSYVSVRKGSLGSSLRGKSPIQDATGKVIGIVSVGYTIEQLENYEKLLE DSLTEITALSIEGREAEHNPVVMVHGIGGASFNFAGIKSYLVSQGWSRDKLYAVDFWDKTGTNYNNGPVLSRFVQKVLDE TGAKKVDIVAHSMGGANTLYYIKNLDGGNKVANVVTLGGANRLTTGKALPGTDPNQKILYTSIYSSADMIVMNYLSRLDG ARNVQIHGVGHIGLLYSSQVNSLIKEGLNGGGQNTN
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experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequencenull
experiment.sample.molecule[0].mw38.495
experiment.sample.molecule[0].total_mw76.99
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.name10 mM glycine buffer, 10 mM NaCl
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
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experiment.sample.buffer.pkanull
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experiment.sample.nameCitrate-binding PAS domain from the sensor histidine kinase, CitA, fused to lipase EstA
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].addressGermany
experiment.contributor[0].affiliation[0].full_nameForschungszentrum Jülich
experiment.contributor[0].affiliation[0].webpagehttps://www.fz-juelich.de
experiment.contributor[0].contributor_nameAndreas
experiment.contributor[0].contributor_surnameStadler
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2014-02-06
experiment.storage_temperature20.0
experiment.cell_temperature20.0
experiment.exposure_time1.0
experiment.number_of_frames10
experiment.wavelength0.09919
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pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionThe protein is a fusion of: i) CitAP - the PAS domain from Sensor histidine kinase, CitA, from Klebsiella pneumoniae; UniProt: P52687 (Amino acid range 45-177); ii) BsLA - the Lipase EstA from Bacillus subtilis 168; UniProt: I6V559 (Amino acid range 32-212) and; iii) A linker connecting CitAP with EstA - derived from the blue light photoreceptor, YtvA, from Bacillus subtilis 168; UniProt: O34627 (Amino acid range 132-147).
experiment_descriptionSynchrotron SAXS data from solutions of the citrate-binding PAS domain from the sensor histidine kinase, CitA, fused to lipase EstA in 10 mM glycine buffer, 10 mM NaCl, pH 10 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.09919 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 4.98 mg/ml was measured at 20°C. 10 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
tags[]
intensity_unitarbitrary
experimental_mw84.42
experimental_mw_errornull
guinier_i0_mw84.42
guinier_i0_mw_error0.068
porod_mwnull
porod_mw_errornull
pddf_i085.43
pddf_i0_errornull
guinier_i084.42
guinier_i0_error0.068
pddf_rg3.423
pddf_rg_errornull
guinier_rg3.32
guinier_rg_error0.06
pddf_dmax11.81
pddf_dmax_errornull
porod_volumenull
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estimated_volumenull
estimated_volume_errornull
guinier_point_first32
guinier_point_last73
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDDJ7_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDDJ7
statussuccess
started_at2026-08-11T15:30:59.204274+00:00
finished_at2026-08-11T15:31:11.794550+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDDJ7",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/nm",
  "project": {
    "title": "A combination of mutational and computational scanning guides the design of an artificial ligand-binding controlled lipase.",
    "publication": {
      "title": "A combination of mutational and computational scanning guides the design of an artificial ligand-binding controlled lipase.",
      "author_list": "Kaschner M, Schillinger O, Fettweiss T, Nutschel C, Krause F, Fulton A, Strodel B, Stadler A, Jaeger KE, Krauss U",
      "journal": "Sci Rep",
      "doi": "10.1038/srep42592",
      "pmid": "28218303",
      "published_date": "2017 Feb 20"
    },
    "status": "released",
    "submitted_date": "2018-05-17",
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            "full_name": "Forschungszentrum Jülich",
            "webpage": "https://www.fz-juelich.de"
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      "fit_residual_plot": "SASDDJ7_fit1_fitresiduals_img.png",
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  "last_modified": "2019-12-06T13:07:15.624532+01:00",
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}
View the complete manifest.json source
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