SASDBY4

Pentameric Nucleoplasmin-histone H2A/H2B complex

Data type: SASBDB experimental data Status: Published Curve type: Merged Last updated: 2021-08-18T17:28:04.360641+02:00

The models displayed for this entry are: Top: ab initio bead model representation (derived from individual reconstructions (example fit shown), aligned, spatially averaged and volume-occupancy corrected): Middle: The best CORAL model using the major A2 site (site #1) of A2:H2A/H2B complex as a starting structure (See Figure 5D in the primary citation). Lacking fragments reconstructed by the program CORAL are shown as spheres. Bottom: The best CORAL model using the minor A2 site (site #2) of A2:H2A/H2B complex as a starting structure (See Figure 5D in the primary citation). Lacking fragments reconstructed by the program CORAL are shown as spheres.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Pentameric Nucleoplasmin-histone H2A/H2B complex

Concentration— – — Buffer / pH20 mM Tris. 150 mM NaCl, 1 mM EDTA, 5 mM DTT / 8.0
Experimental temperature20.0 Facility / beamlineStanford Synchrotron Radiation Lightsource (SSRL) / BL4-2
Wavelength0.1127 nmExposure1.0 s × 55

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Nucleoplasmin core + A2
View sequence
ASTASNTSKVEKPVSLIWGCELNEQNKTFAFKIEDEEEKCEHQLALRTVCLGDKAKDEFHIVEIVTQEEGKEKPVPIASLKPSILPMATMVGIELTPPVTFRLKAGSGPVYISGQHVAMEEDYSWAEEEDEGEEEEEEEEDPESP
proteinXenopus laevisQ6NUC72–145pentamerMolecule count 516.165 kDa
Histone H2A (ΔAla127)
View sequence
SGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKTESSKSKSK
proteinXenopus laevisQ6AZJ82–130pentamerMolecule count 513.879 kDa
Histone H2B 1.1 (Ser33Thr)
View sequence
AKSAPAPKKGSKKAVTKTQKKDGKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK
proteinXenopus laevisP022815–126pentamerMolecule count 513.494 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1311[3]0.160046–2.99363 1/nmHas uncertainty columnMissing 00sasbdb/entries/y4/sasdby4/source/SASDBY4.dat
▼

2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)14.0—nm
i0Guinier2875.5214.75—
i0P(r)2822.08.0—
mwExperimental251.0—kDa
porod_volumePorod402.0—nm³
rgGuinier4.390.03nm
rgP(r)4.320.01nm

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 name20 mM Tris. 150 mM NaCl, 1 mM EDTA, 5 mM DTTBuffer concentration20.0 mM
pH8.0Additives150mM NaCl, 1mM EDTA, 5mM DTT
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2016-01-07Storage / measurement temperature20.0 / 20.0
Exposure time1.0Frames55
Wavelength0.1127Sample-to-detector distance1.7
SourceX-ray synchrotronDetectorRayonix MX225-HE
Facility / beamlineStanford Synchrotron Radiation Lightsource (SSRL) / BL4-2 · Menlo Park, CA, USA
q range0.16 – 2.994Sample 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:264 field values
Field pathRaw value
codeSASDBY4
statusPublished
type_of_curveMerged
angular_unit1/nm
project.titleDynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release.
project.publication.titleDynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release.
project.publication.author_listWarren C, Matsui T, Karp JM, Onikubo T, Cahill S, Brenowitz M, Cowburn D, Girvin M, Shechter D
project.publication.journalNat Commun
project.publication.doi10.1038/s41467-017-02308-3
project.publication.pmid29263320
project.publication.published_date2017 Dec 20
project.statusreleased
project.submitted_date2016-06-02
project.released_date2017-11-18
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDBY4.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDBY4.dat
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intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDBY4_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDBY4_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDBY4_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDBY4.sascif
experiment.instrument.detector.typenull
experiment.instrument.detector.nameRayonix MX225-HE
experiment.instrument.detector.resolutionnull
experiment.instrument.nameStanford Synchrotron Radiation Lightsource (SSRL)
experiment.instrument.cityMenlo Park, CA
experiment.instrument.countryUSA
experiment.instrument.beamline_nameBL4-2
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_nameNucleoplasmin core + A2
experiment.sample.molecule[0].short_nameNpm core
experiment.sample.molecule[0].sequenceASTASNTSKVEKPVSLIWGCELNEQNKTFAFKIEDEEEKCEHQLALRTVCLGDKAKDEFHIVEIVTQEEGKEKPVPIASLKPSILPMATMVGIELTPPVTFRLKAGSGPVYISGQHVAMEEDYSWAEEEDEGEEEEEEEEDPESP
experiment.sample.molecule[0].organismXenopus laevis
experiment.sample.molecule[0].uniprot_codeQ6NUC7
experiment.sample.molecule[0].uniprot_range_first2
experiment.sample.molecule[0].uniprot_range_last145
experiment.sample.molecule[0].oligomerizationpentamer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequencenull
experiment.sample.molecule[0].mw16.165
experiment.sample.molecule[0].total_mw80.824
experiment.sample.molecule[0].number_molecules5
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_nameHistone H2A (ΔAla127)
experiment.sample.molecule[1].short_name2HA
experiment.sample.molecule[1].sequenceSGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKTESSKSKSK
experiment.sample.molecule[1].organismXenopus laevis
experiment.sample.molecule[1].uniprot_codeQ6AZJ8
experiment.sample.molecule[1].uniprot_range_first2
experiment.sample.molecule[1].uniprot_range_last130
experiment.sample.molecule[1].oligomerizationpentamer
experiment.sample.molecule[1].molecular_typeprotein
experiment.sample.molecule[1].uniprot_sequenceMSGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLT AEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKK TESSKSAKSK
experiment.sample.molecule[1].mw13.879
experiment.sample.molecule[1].total_mw69.395
experiment.sample.molecule[1].number_molecules5
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.molecule[2].long_nameHistone H2B 1.1 (Ser33Thr)
experiment.sample.molecule[2].short_nameH2B
experiment.sample.molecule[2].sequenceAKSAPAPKKGSKKAVTKTQKKDGKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK
experiment.sample.molecule[2].organismXenopus laevis
experiment.sample.molecule[2].uniprot_codeP02281
experiment.sample.molecule[2].uniprot_range_first5
experiment.sample.molecule[2].uniprot_range_last126
experiment.sample.molecule[2].oligomerizationpentamer
experiment.sample.molecule[2].molecular_typeprotein
experiment.sample.molecule[2].uniprot_sequenceMPEPAKSAPAPKKGSKKAVTKTQKKDGKKRRKSRKESYAIYVYKVLKQVHPDTGISSKAM SIMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVT KYTSAK
experiment.sample.molecule[2].mw13.494
experiment.sample.molecule[2].total_mw67.468
experiment.sample.molecule[2].number_molecules5
experiment.sample.molecule[2].complex_stateFalse
experiment.sample.molecule[2].deuterationnull
experiment.sample.molecule[2].molecule_sourcebiological
experiment.sample.molecule[2].molecule_descriptionnull
experiment.sample.buffer.name20 mM Tris. 150 mM NaCl, 1 mM EDTA, 5 mM DTT
experiment.sample.buffer.concentration_unitmM
experiment.sample.buffer.commentnull
experiment.sample.buffer.additive150mM NaCl, 1mM EDTA, 5mM DTT
experiment.sample.buffer.concentration20.0
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph8.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.namePentameric Nucleoplasmin-histone H2A/H2B 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[]
experiment.contributor[0].contributor_nameMichael
experiment.contributor[0].contributor_surnameBrenowitz
experiment.contributor[0].orcidnull
experiment.contributor[1].affiliation[]
experiment.contributor[1].contributor_nameSean
experiment.contributor[1].contributor_surnameCahill
experiment.contributor[1].orcidnull
experiment.contributor[2].affiliation[]
experiment.contributor[2].contributor_nameMark
experiment.contributor[2].contributor_surnameGirvin
experiment.contributor[2].orcidnull
experiment.contributor[3].affiliation[]
experiment.contributor[3].contributor_nameJerome
experiment.contributor[3].contributor_surnameKarp
experiment.contributor[3].orcidnull
experiment.contributor[4].affiliation[0].short_nameSLAC
experiment.contributor[4].affiliation[0].addressMenlo Park, CA, USA
experiment.contributor[4].affiliation[0].full_nameStanford Synchrotron Radiation Lightsource
experiment.contributor[4].affiliation[0].webpagehttp://www-ssrl.slac.stanford.edu/
experiment.contributor[4].contributor_nameTsutomu
experiment.contributor[4].contributor_surnameMatsui
experiment.contributor[4].orcidnull
experiment.contributor[5].affiliation[]
experiment.contributor[5].contributor_nameTakashi
experiment.contributor[5].contributor_surnameOnikubo
experiment.contributor[5].orcidnull
experiment.contributor[6].affiliation[]
experiment.contributor[6].contributor_nameDavid
experiment.contributor[6].contributor_surnameShechter
experiment.contributor[6].orcidnull
experiment.contributor[7].affiliation[]
experiment.contributor[7].contributor_nameChristopher
experiment.contributor[7].contributor_surnameWarren
experiment.contributor[7].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2016-01-07
experiment.storage_temperature20.0
experiment.cell_temperature20.0
experiment.exposure_time1.0
experiment.number_of_frames55
experiment.wavelength0.1127
experiment.sample_detector_distance1.7
experiment.concentration_minnull
experiment.concentration_maxnull
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.16
experiment.s_max2.994
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].lognull
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fits[0].models[0].user131
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fits[0].softwarenull
fits[0].chi_square_value1.58
fits[0].p_value0.0
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fits[2].p_value0.000139
fits[2].fit_residual_plotMinor_site_fitresiduals_img.png
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fits[2].fit_lognull
fits[2].software_versionnull
fits[2].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionnull
i0_calibration_standardnull
descriptionThe models displayed for this entry are: Top: ab initio bead model representation (derived from individual reconstructions (example fit shown), aligned, spatially averaged and volume-occupancy corrected): Middle: The best CORAL model using the major A2 site (site #1) of A2:H2A/H2B complex as a starting structure (See Figure 5D in the primary citation). Lacking fragments reconstructed by the program CORAL are shown as spheres. Bottom: The best CORAL model using the minor A2 site (site #2) of A2:H2A/H2B complex as a starting structure (See Figure 5D in the primary citation). Lacking fragments reconstructed by the program CORAL are shown as spheres.
experiment_descriptionSynchrotron SAXS data measured from solutions of the pentameric nucleoplasmin-histone H2A/H2B complex in 20 mM Tris 150mM NaCl, 1mM EDTA, 5mM DTT, pH 8.0, were collected on the BL4-2 beam line at the Stanford Synchrotron Radiation Lightsource (Stanford, USA) using a Rayonix MX225-HE detector (I(s) vs s; s = 4π sin θ/λ, where 2θ is the scattering angle and λ=0.1127 nm). Fifty five successive 1 s data frames were collected immediately after the protein complex eluted from a size-exclusion chromatography (SEC) column. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank (derived from the SEC running solvent) was subtracted and the individual solvent-corrected SAXS profiles were scaled and averaged to produce the final merged SAXS data profile.
tags[]
intensity_unitnull
experimental_mw251.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_error251.0
pddf_i02822.0
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View the complete summary.json source
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  "angular_unit": "1/nm",
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    "title": "Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release.",
    "publication": {
      "title": "Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release.",
      "author_list": "Warren C, Matsui T, Karp JM, Onikubo T, Cahill S, Brenowitz M, Cowburn D, Girvin M, Shechter D",
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      "doi": "10.1038/s41467-017-02308-3",
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View the complete manifest.json source
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