SASDXW7

Kinase domain of Aurora kinase A mutant C290A:C393A

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2026-02-25T14:53:48.895959+01:00

Synchrotron SAXS data from solutions of the kinase domain of Aurora kinase A (residues 122-403, containing a C290A:C393A double mutation) was collected in 20mM HEPES, 150mM NaCl, 5mM MgCl2, 3% v/v glycerol, 2mM TCEP, pH 7.5 on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAXS was employed by injecting 80.00 μl sample of 14 mg/ml onto a GE Superdex 75 Increase 10/300 column with a flow rate of 0.70 ml/min at 20°C. 2100 successive 1 second frames were collected. The data was normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. Buffer subtraction was done using CHROMIXS and data analysis was done using the ATSAS suite. The experimental molecular weight was also determined from SEC-MALLS run in parallel to SEC-SAXS.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Kinase domain of Aurora kinase A mutant C290A:C393A

Concentration— – — Buffer / pH20mM HEPES, 150mM NaCl, 5mM MgCl2, 3% v/v glycerol, 2mM TCEP / 7.5
Experimental temperature— Facility / beamlinePETRA III / EMBL P12
Wavelength— nmExposure— s × —

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Aurora kinase A mutant C290A:C393A
View sequence
ESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLAGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWITANSSKPSNAQNKESASKQS
proteinHomo sapiensO14965122–403monomerMolecule count 132.573 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
12617[3]0.0223001–7.31442 1/nmHas uncertainty columnMissing 014sasbdb/entries/w7/sasdxw7/source/SASDXW7.dat
▼

2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)9.5—nm
i0Guinier0.0466382—1/cm
i0P(r)0.04688—1/cm
mwExperimental29.6—kDa
mwPorod37.0—kDa
porod_volumePorod59.05—nm³
rgGuinier2.220.005nm
rgP(r)2.279—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

This entry has no source fit record.

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4. Source File Index Source Files

▶

5. Experiment Description and Publication Experiment & Publication

▼

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 name20mM HEPES, 150mM NaCl, 5mM MgCl2, 3% v/v glycerol, 2mM TCEPBuffer concentration—
pH7.5Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2023-11-28Storage / measurement temperature— / —
Exposure time—Frames—
Wavelength—Sample-to-detector distance—
SourceX-ray synchrotronDetectorPilatus 6M
Facility / beamlinePETRA III / EMBL P12 · DESY; Hamburg, Germany
q range0.022 – 7.314Sample volume / flow rate90.0 / 0.7

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:134 field values
Field pathRaw value
codeSASDXW7
statusPublished
type_of_curveSingle concentration
angular_unit1/nm
project.titleThe N-Myc MB0-MBI region interacts specifically and dynamically with the N-lobe of Aurora kinase A.
project.publication.titleThe N-Myc MB0-MBI region interacts specifically and dynamically with the N-lobe of Aurora kinase A.
project.publication.author_listHultman J, Morad V, Tanner E, Kenney TMG, Pietras Z, Khare LP, Derbyshire D, Resetca D, Arrowsmith CH, Aili D, Ekström S, Penn LZ, Wallner B, Ahlner A, Sunnerhagen M
project.publication.journalNat Commun
project.publication.doi10.1038/s41467-026-69725-1
project.publication.pmid41735282
project.publication.published_date2026 Feb 24
project.statusreleased
project.submitted_date2025-08-19
project.released_date2026-01-30
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experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus 6M
experiment.instrument.detector.resolutionnull
experiment.instrument.namePETRA III
experiment.instrument.cityDESY; Hamburg
experiment.instrument.countryGermany
experiment.instrument.beamline_nameEMBL P12
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_nameAurora kinase A mutant C290A:C393A
experiment.sample.molecule[0].short_nameAurA C290A:C393A
experiment.sample.molecule[0].sequenceESKKRQWALE DFEIGRPLGK GKFGNVYLAR EKQSKFILAL KVLFKAQLEK AGVEHQLRRE VEIQSHLRHP NILRLYGYFH DATRVYLILE YAPLGTVYRE LQKLSKFDEQ RTATYITELA NALSYCHSKR VIHRDIKPEN LLLGSAGELK IADFGWSVHA PSSRRTTLAG TLDYLPPEMI EGRMHDEKVD LWSLGVLCYE FLVGKPPFEA NTYQETYKRI SRVEFTFPDF VTEGARDLIS RLLKHNPSQR PMLREVLEHP WITANSSKPS NAQNKESASK QS
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeO14965
experiment.sample.molecule[0].uniprot_range_first122
experiment.sample.molecule[0].uniprot_range_last403
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRIPLQ AQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSAPENNPEEELASKQKN EESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRR EVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITEL ANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEM IEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLI SRLLKHNPSQRPMLREVLEHPWITANSSKPSNCQNKESASKQS
experiment.sample.molecule[0].mw32.573
experiment.sample.molecule[0].total_mw32.573
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_description
experiment.sample.buffer.name20mM HEPES, 150mM NaCl, 5mM MgCl2, 3% v/v glycerol, 2mM TCEP
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.nameKinase domain of Aurora kinase A mutant C290A:C393A
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].addressnull
experiment.contributor[0].affiliation[0].full_nameLinköping University
experiment.contributor[0].affiliation[0].webpagenull
experiment.contributor[0].contributor_nameJohanna
experiment.contributor[0].contributor_surnameHultman
experiment.contributor[0].orcidhttps://orcid.org/0009-0000-8066-228X
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2023-11-28
experiment.storage_temperaturenull
experiment.cell_temperaturenull
experiment.exposure_timenull
experiment.number_of_framesnull
experiment.wavelengthnull
experiment.sample_detector_distancenull
experiment.concentration_minnull
experiment.concentration_maxnull
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experiment.flow_rate0.7
experiment.s_min0.022
experiment.s_max7.314
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionSynchrotron SAXS data from solutions of the kinase domain of Aurora kinase A (residues 122-403, containing a C290A:C393A double mutation) was collected in 20mM HEPES, 150mM NaCl, 5mM MgCl2, 3% v/v glycerol, 2mM TCEP, pH 7.5 on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAXS was employed by injecting 80.00 μl sample of 14 mg/ml onto a GE Superdex 75 Increase 10/300 column with a flow rate of 0.70 ml/min at 20°C. 2100 successive 1 second frames were collected. The data was normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. Buffer subtraction was done using CHROMIXS and data analysis was done using the ATSAS suite. The experimental molecular weight was also determined from SEC-MALLS run in parallel to SEC-SAXS.
experiment_descriptionnull
tags[]
intensity_unit1/cm
experimental_mw29.6
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw37.0
porod_mw_errornull
pddf_i00.04688
pddf_i0_errornull
guinier_i00.0466382
guinier_i0_errornull
pddf_rg2.279
pddf_rg_errornull
guinier_rg2.22
guinier_rg_error0.005
pddf_dmax9.5
pddf_dmax_errornull
porod_volume59.05
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first35
guinier_point_last202
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDXW7_datloglog_img.png
symmetrynull
last_modified2026-02-25T14:53:48.895959+01:00
bragg_peak[]
manifest.json:34 field values
Field pathRaw value
codeSASDXW7
statussuccess
started_at2026-08-11T15:41:40.780879+00:00
finished_at2026-08-11T15:41:49.807781+00:00
source_last_modified2026-02-25T14:53:48.895959+01:00
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View the complete summary.json source
{
  "code": "SASDXW7",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/nm",
  "project": {
    "title": "The N-Myc MB0-MBI region interacts specifically and dynamically with the N-lobe of Aurora kinase A.",
    "publication": {
      "title": "The N-Myc MB0-MBI region interacts specifically and dynamically with the N-lobe of Aurora kinase A.",
      "author_list": "Hultman J, Morad V, Tanner E, Kenney TMG, Pietras Z, Khare LP, Derbyshire D, Resetca D, Arrowsmith CH, Aili D, Ekström S, Penn LZ, Wallner B, Ahlner A, Sunnerhagen M",
      "journal": "Nat Commun",
      "doi": "10.1038/s41467-026-69725-1",
      "pmid": "41735282",
      "published_date": "2026 Feb 24"
    },
    "status": "released",
    "submitted_date": "2025-08-19",
    "released_date": "2026-01-30"
  },
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          "long_name": "Aurora kinase A mutant C290A:C393A",
          "short_name": "AurA C290A:C393A",
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  "last_modified": "2026-02-25T14:53:48.895959+01:00",
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View the complete manifest.json source
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