SASDCZ4

RNase E 603-850/ATP-dependent RNA helicase (RhlB) binary complex

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

Sample 1 · RNase E 603-850/ATP-dependent RNA helicase (RhlB) binary complex

Concentration— – 22.3 Buffer / pH50 mM Tris HCl, 100 mM NaCl, 100 mM KCl, 10 mM MgCl2, 10 mM DTT and 5 % glycerol (v/v) / 7.5
Experimental temperature15.0 Facility / beamlineSOLEIL / SWING
Wavelength0.1022 nmExposure1.5 s × 250

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
RNase E 603-850
View sequence
ERQQDRRKPRQNNRRDRNERRDTRSERTEGSDNREENRRNRRQAQQQTAETRESRQQAEVTEKARTADEQQAPRRERSRRRNDDKRQAQQEAKALNVEEQSVQETEQEERVRPVQPRRKQRQLNQKVRYEQSVAEEAVVAPVVEETVAAEPIVQEAPAPRTELVKVPLPVVAQTAPEQQEENNADNRDNGGMPRRSRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPELASGKVWIRYPIVRHHHHHH
proteinEscherichia coliQ46977603–850monomerMolecule count 130.127 kDa
ATP-dependent RNA helicase RhlB
View sequence
MSKTHLTEQKFSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIADRKVNQPRALIMAPTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKDIRWLFRRMPPANQRLNMLFSATLSYRVRELAFEQMNNAEYIEVEPEQKTGHRIKEELFYPSNEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSIPVSKYNPDALMTDLPKPLRLTRPRTGNGPRRTGAPRNRRRSG
proteinEscherichia coliW8ZZD41–421monomerMolecule count 147.125 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11080[3]0.006219606–0.6139486 1/AHas uncertainty columnMissing 02sasbdb/entries/z4/sasdcz4/source/SASDCZ4.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)29.51.0Å
i0Guinier0.21720.01—
i0P(r)0.2172580.01—
mwExperimental139.0—kDa
mwPorod107.7—kDa
porod_volumePorod183.0—ų
rgGuinier5.3750.071Å
rgP(r)5.8750.015Å

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 HCl, 100 mM NaCl, 100 mM KCl, 10 mM MgCl2, 10 mM DTT and 5 % glycerol (v/v)Buffer concentration—
pH7.5Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2016-02-11Storage / measurement temperature15.0 / 15.0
Exposure time1.5Frames250
Wavelength0.1022Sample-to-detector distance1.79
SourceX-ray synchrotronDetectorAVIEX PCCD170170
Facility / beamlineSOLEIL / SWING · Saint-Aubin, France
q range0.062 – 6.139Sample 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 (4 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:173 field values
Field pathRaw value
codeSASDCZ4
statusPublished
type_of_curveOther
angular_unit1/A
project.titleAnalysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes.
project.publication.titleAnalysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes.
project.publication.author_listBruce HA, Du D, Matak-Vinkovic D, Bandyra KJ, Broadhurst RW, Martin E, Sobott F, Shkumatov AV, Luisi BF
project.publication.journalNucleic Acids Res
project.publication.doi10.1093/nar/gkx1083
project.publication.pmid29136196
project.publication.published_date2018 Jan 9
project.statusreleased
project.submitted_date2017-06-07
project.released_date2017-11-09
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDCZ4.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDCZ4.dat
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sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDCZ4.sascif
experiment.instrument.detector.typeCCD
experiment.instrument.detector.nameAVIEX PCCD170170
experiment.instrument.detector.resolutionnull
experiment.instrument.nameSOLEIL
experiment.instrument.citySaint-Aubin
experiment.instrument.countryFrance
experiment.instrument.beamline_nameSWING
experiment.instrument.beam_geometry
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_nameRNase E 603-850
experiment.sample.molecule[0].short_nameRNase E 603-850
experiment.sample.molecule[0].sequenceERQQDRRKPRQNNRRDRNERRDTRSERTEGSDNREENRRNRRQAQQQTAETRESRQQA EVTEKARTADEQQAPRRERSRRRNDDKRQAQQEAKALNVEEQSVQETEQEERVRPVQPRR KQRQLNQKVRYEQSVAEEAVVAPVVEETVAAEPIVQEAPAPRTELVKVPLPVVAQTAPEQ QEENNADNRDNGGMPRRSRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPELASG KVWIRYPIVRHHHHHH
experiment.sample.molecule[0].organismEscherichia coli
experiment.sample.molecule[0].uniprot_codeQ46977
experiment.sample.molecule[0].uniprot_range_first603
experiment.sample.molecule[0].uniprot_range_last850
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceLSYMLPKLHEEAMALPSEEEFAERKRPEQPALATFAMPDVPPAPTPAEPAAPVVAPAPKA APATPAAPAQPGLLSRFFGALKALFSGGEETKPTEQPAPKAEAKPERQQDRRKPRQNNRR DRNERRDTRSERTEGSDNREENRRNRRQAQQQTAETRESRQQAEVTEKARTADEQQAPRR ERSRRRNDDKRQAQQEAKALNVEEQSVQETEQEERVRPVQPRRKQRQLNQKVRYEQSVAE EAVVAPVVEETVAAEPIVQEAPAPRTELVKVPLPVVAQTAPEQQEENNADNRDNGGMPRR SRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPELASGKVWIRYPIVRPQDVQVE EQREQEEVHVQPMVTEVPVAAAIEPVVSAPVVEEVAGVVEAPVQVAEPQPEVVETTHPEV IAAAVTEQPQVITESDVAVAQEVAEQAEPVVEPQEETADIEEVVETAEVVVAEPEVVAQP AAPVVAEVAAEVETVAAVEPEVTVEHNHATAPMTRAPAPEYVPEAPRHSDWQRPTFA
experiment.sample.molecule[0].mw30.127
experiment.sample.molecule[0].total_mw30.127
experiment.sample.molecule[0].number_molecules1
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.molecule[1].long_nameATP-dependent RNA helicase RhlB
experiment.sample.molecule[1].short_nameRhlB
experiment.sample.molecule[1].sequenceMSKTHLTEQKFSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKT MAFLTSTFHYLLSHPAIADRKVNQPRALIMAPTRELAVQIHADAEPLAEATGLKLGLAYG GDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKDIR WLFRRMPPANQRLNMLFSATLSYRVRELAFEQMNNAEYIEVEPEQKTGHRIKEELFYPSN EEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILD EFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLA CEEYALNLPAIETYIGHSIPVSKYNPDALMTDLPKPLRLTRPRTGNGPRRTGAPRNRRRS G
experiment.sample.molecule[1].organismEscherichia coli
experiment.sample.molecule[1].uniprot_codeW8ZZD4
experiment.sample.molecule[1].uniprot_range_first1
experiment.sample.molecule[1].uniprot_range_last421
experiment.sample.molecule[1].oligomerizationmonomer
experiment.sample.molecule[1].molecular_typeprotein
experiment.sample.molecule[1].uniprot_sequenceMSKTHLTEQKFSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKT MAFLTSTFHYLLSHPAIADRKVNQPRALIMAPTRELAVQIHADAEPLAEATGLKLGLAYG GDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKDIR WLFRRMPPANQRLNMLFSATLSYRVRELAFEQMNNAEYIEVEPEQKTGHRIKEELFYPSN EEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILD EFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLA CEEYALNLPAIETYIGHSIPVSKYNPDALMTDLPKPLRLTRPRTGNGPRRTGAPRNRRRS G
experiment.sample.molecule[1].mw47.125
experiment.sample.molecule[1].total_mw47.125
experiment.sample.molecule[1].number_molecules1
experiment.sample.molecule[1].complex_stateFalse
experiment.sample.molecule[1].deuterationnull
experiment.sample.molecule[1].molecule_sourcebiological
experiment.sample.molecule[1].molecule_descriptionnull
experiment.sample.buffer.name50 mM Tris HCl, 100 mM NaCl, 100 mM KCl, 10 mM MgCl2, 10 mM DTT and 5 % glycerol (v/v)
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameRNase E 603-850/ATP-dependent RNA helicase (RhlB) binary complex
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_nameVUB
experiment.contributor[0].affiliation[0].addressPleinlaan 2 1050 Brussel
experiment.contributor[0].affiliation[0].full_nameVrije Universiteit Brussel
experiment.contributor[0].affiliation[0].webpagehttp://www.vub.ac.be/
experiment.contributor[0].contributor_nameAlexander
experiment.contributor[0].contributor_surnameShkumatov
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2016-02-11
experiment.storage_temperature15.0
experiment.cell_temperature15.0
experiment.exposure_time1.5
experiment.number_of_frames250
experiment.wavelength0.1022
experiment.sample_detector_distance1.79
experiment.concentration_minnull
experiment.concentration_max22.3
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.062
experiment.s_max6.139
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].bead_radius1.9
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fits[0].models[0].symmetryP1
fits[0].models[0].commentBest fitting model out of 10 independent reconstructions
fits[0].models[0].user104
fits[0].fit_unit1/A
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fits[0].softwareGASBOR
fits[0].chi_square_value16.39
fits[0].p_value1e-06
fits[0].fit_residual_plotSASDCZ4_fit1_fitresiduals_img.png
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fits[0].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionv5.0 (r8972)
i0_calibration_standardnull
descriptionnull
experiment_descriptionSAXS data (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle) were collected on the SWING beam ine at the Soleil synchrotron (Gif-sur-Yvette, France). Samples were stored at 288 K in a robotic sample chamber and automatically loaded (22.3 mg/ml) onto a Superdex 200 Increase 3.2/300 gel-filtration column (GE Healthcare) equilibrated with 50 mM Tris HCl pH 7.5, 100 mM NaCl, 100 mM KCl, 10 mM MgCl2, 10 mM DTT and 5 % glycerol (v/v), at a flow rate of 150 μl min-1 by a HPLC (High performance liquid chromatography) instrument (Agilent), directly before elution into the sample detection chamber, where a monochromatic beam illuminated the sample with a wavelength of 0.1022 nm as it flowed through. The sample-detector distance was 1.79 m. During the elution, 250 scattering measurements were taken with 1.5-s time-frames and 0.5-s dead-time between frames. The in-house program FOXTROT (David and Pérez, 2009) was used to normalize and radially average the data. After averaging 20-30 buffer frames in PRIMUS (Konarev et al., 2003), the program DATASW (Shkumatov and Strelkov, 2015) was employed to (i) subtract the buffer average from each sample frame and (ii) calculation of I(0), Rg and MW. Frames corresponding to the peak where Rg was stable were used for averaging.
tags[]
intensity_unitnull
experimental_mw139.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw107.7
porod_mw_errornull
pddf_i00.217258
pddf_i0_error0.01
guinier_i00.2172
guinier_i0_error0.01
pddf_rg5.875
pddf_rg_error0.015
guinier_rg5.375
guinier_rg_error0.071
pddf_dmax29.5
pddf_dmax_error1.0
porod_volume183.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first8
guinier_point_last25
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDCZ4_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDCZ4
statussuccess
started_at2026-08-11T14:34:59.820897+00:00
finished_at2026-08-11T14:35:12.081526+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDCZ4",
  "status": "Published",
  "type_of_curve": "Other",
  "angular_unit": "1/A",
  "project": {
    "title": "Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes.",
    "publication": {
      "title": "Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes.",
      "author_list": "Bruce HA, Du D, Matak-Vinkovic D, Bandyra KJ, Broadhurst RW, Martin E, Sobott F, Shkumatov AV, Luisi BF",
      "journal": "Nucleic Acids Res",
      "doi": "10.1093/nar/gkx1083",
      "pmid": "29136196",
      "published_date": "2018 Jan 9"
    },
    "status": "released",
    "submitted_date": "2017-06-07",
    "released_date": "2017-11-09"
  },
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View the complete manifest.json source
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