SASDBY7

N-terminal and chromo-ATPase domains of chromo domain-containing protein 1 (Chd1: 1-1010)

Data type: SASBDB experimental data Status: Published Curve type: Extrapolated to infinite dilution Last updated: 2023-05-25T11:22:08.798758+02:00

The protein fragment 1-1010 encompassing the N-terminal and chromo-ATPase domains of Saccharomyces cerevisiae Chd1.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · N-terminal and chromo-ATPase domains of chromo domain-containing protein 1 (Chd1: 1-1010)

Concentration0.6 – 9.8 Buffer / pH50mM Hepes 150mM NaCl / 7.5
Experimental temperature10.0 Facility / beamlineDORIS III, DESY / EMBL X33
Wavelength0.154 nmExposure120.0 s × —

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
chromodomain helicase DNA binding domain
View sequence
MAAKDISTEVLQNPELYGLRRSHRAAAHQQNYFNDSDDEDDEDNIKQSRRKRMTTIEDDEDEFEDEEGEEDSGEDEDEEDFEEDDDYYGSPIKQNRSKPKSRTKSKSKSKPKSQSEKQSTVKIPTRFSNRQNKTVNYNIDYSDDDLLESEDDYGSEEALSEENVHEASANPQPEDFHGIDIVINHRLKTSLEEGKVLEKTVPDLNNCKENYEFLIKWTDESHLHNTWETYESIGQVRGLKRLDNYCKQFIIEDQQVRLDPYVTAEDIEIMDMERERRLDEFEEFHVPERIIDSQRASLEDGTSQLQYLVKWRRLNYDEATWENATDIVKLAPEQVKHFQNRENSKILPQYSSNYTSQRPRFEKLSVQPPFIKGGELRDFQLTGINWMAFLWSKGDNGILADEMGLGKTVQTVAFISWLIFARRQNGPHIIVVPLSTMPAWLDTFEKWAPDLNCICYMGNQKSRDTIREYEFYTNPRAKGKKTMKFNVLLTTYEYILKDRAELGSIKWQFMAVDEAHRLKNAESSLYESLNSFKVANRMLITGTPLQNNIKELAALVNFLMPGRFTIDQEIDFENQDEEQEEYIHDLHRRIQPFILRRLKKDVEKSLPSKTERILRVELSDVQTEYYKNILTKNYSALTAGAKGGHFSLLNIMNELKKASNHPYLFDNAEERVLQKFGDGKMTRENVLRGLIMSSGKMVLLDQLLTRLKKDGHRVLIFSQMVRMLDILGDYLSIKGINFQRLDGTVPSAQRRISIDHFNSPDSNDFVFLLSTRAGGLGINLMTADTVVIFDSDWNPQADLQAMARAHRIGQKNHVMVYRLVSKDTVEEEVLERARKKMILEYAIISLGVTDGNKYTKKNEPNAGELSAILKFGAGNMFTATDNQKKLEDLNLDDVLNHAEDHVTTPDLGESHLGGEEFLKQFEVTDYKADIDWDDIIPEEELKKLQDEEQKRKDEEYVKEQLEMMNRRDNALKKIKNSVNGDGTAANSDSDDDSTSRSSRRRARANDMDSI
proteinSaccharomyces cerevisiaeP326571–1010monomerMolecule count 1116.922 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
12083[3]0.07307–4.945 1/nmHas uncertainty columnMissing 0620sasbdb/entries/y7/sasdby7/source/SASDBY7.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)12.0—nm
i0Guinier1.360.0035—
i0P(r)1.220.001—
mwExperimental120.0—kDa
porod_volumePorod228.0—nm³
rgGuinier4.530.01nm
rgP(r)4.070.002nm

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 name50mM Hepes 150mM NaClBuffer concentration—
pH7.5Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2008-11-30Storage / measurement temperature10.0 / 10.0
Exposure time120.0Frames—
Wavelength0.154Sample-to-detector distance5.0
SourceX-ray synchrotronDetectorPilatus 2M
Facility / beamlineDORIS III, DESY / EMBL X33 · Hamburg, Germany
q range0.073 – 4.945Sample 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:156 field values
Field pathRaw value
codeSASDBY7
statusPublished
type_of_curveExtrapolated to infinite dilution
angular_unit1/nm
project.titleStructural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes.
project.publication.titleStructural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes.
project.publication.author_listSundaramoorthy R, Hughes AL, Singh V, Wiechens N, Ryan DP, El-Mkami H, Petoukhov M, Svergun DI, Treutlein B, Quack S, Fischer M, Michaelis J, Böttcher B, Norman DG, Owen-Hughes T
project.publication.journalElife
project.publication.doi10.7554/eLife.22510
project.publication.pmid28332978
project.publication.published_date2017 Mar 23
project.statusreleased
project.submitted_date2016-11-26
project.released_date2017-05-02
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDBY7.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDBY7.dat
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experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus 2M
experiment.instrument.detector.resolutionnull
experiment.instrument.nameDORIS III, DESY
experiment.instrument.cityHamburg
experiment.instrument.countryGermany
experiment.instrument.beamline_nameEMBL X33
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_namechromodomain helicase DNA binding domain
experiment.sample.molecule[0].short_nameChd1
experiment.sample.molecule[0].sequenceMAAKDISTEV LQNPELYGLR RSHRAAAHQQ NYFNDSDDED DEDNIKQSRR KRMTTIEDDE DEFEDEEGEE DSGEDEDEED FEEDDDYYGS PIKQNRSKPK SRTKSKSKSK PKSQSEKQST VKIPTRFSNR QNKTVNYNID YSDDDLLESE DDYGSEEALS EENVHEASAN PQPEDFHGID IVINHRLKTS LEEGKVLEKT VPDLNNCKEN YEFLIKWTDE SHLHNTWETY ESIGQVRGLK RLDNYCKQFI IEDQQVRLDP YVTAEDIEIM DMERERRLDE FEEFHVPERI IDSQRASLED GTSQLQYLVK WRRLNYDEAT WENATDIVKL APEQVKHFQN RENSKILPQY SSNYTSQRPR FEKLSVQPPF IKGGELRDFQ LTGINWMAFL WSKGDNGILA DEMGLGKTVQ TVAFISWLIF ARRQNGPHII VVPLSTMPAW LDTFEKWAPD LNCICYMGNQ KSRDTIREYE FYTNPRAKGK KTMKFNVLLT TYEYILKDRA ELGSIKWQFM AVDEAHRLKN AESSLYESLN SFKVANRMLI TGTPLQNNIK ELAALVNFLM PGRFTIDQEI DFENQDEEQE EYIHDLHRRI QPFILRRLKK DVEKSLPSKT ERILRVELSD VQTEYYKNIL TKNYSALTAG AKGGHFSLLN IMNELKKASN HPYLFDNAEE RVLQKFGDGK MTRENVLRGL IMSSGKMVLL DQLLTRLKKD GHRVLIFSQM VRMLDILGDY LSIKGINFQR LDGTVPSAQR RISIDHFNSP DSNDFVFLLS TRAGGLGINL MTADTVVIFD SDWNPQADLQ AMARAHRIGQ KNHVMVYRLV SKDTVEEEVL ERARKKMILE YAIISLGVTD GNKYTKKNEP NAGELSAILK FGAGNMFTAT DNQKKLEDLN LDDVLNHAED HVTTPDLGES HLGGEEFLKQ FEVTDYKADI DWDDIIPEEE LKKLQDEEQK RKDEEYVKEQ LEMMNRRDNA LKKIKNSVNG DGTAANSDSD DDSTSRSSRR RARANDMDSI
experiment.sample.molecule[0].organismSaccharomyces cerevisiae
experiment.sample.molecule[0].uniprot_codeP32657
experiment.sample.molecule[0].uniprot_range_first1
experiment.sample.molecule[0].uniprot_range_last1010
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMAAKDISTEVLQNPELYGLRRSHRAAAHQQNYFNDSDDEDDEDNIKQSRRKRMTTIEDDE DEFEDEEGEEDSGEDEDEEDFEEDDDYYGSPIKQNRSKPKSRTKSKSKSKPKSQSEKQST VKIPTRFSNRQNKTVNYNIDYSDDDLLESEDDYGSEEALSEENVHEASANPQPEDFHGID IVINHRLKTSLEEGKVLEKTVPDLNNCKENYEFLIKWTDESHLHNTWETYESIGQVRGLK RLDNYCKQFIIEDQQVRLDPYVTAEDIEIMDMERERRLDEFEEFHVPERIIDSQRASLED GTSQLQYLVKWRRLNYDEATWENATDIVKLAPEQVKHFQNRENSKILPQYSSNYTSQRPR FEKLSVQPPFIKGGELRDFQLTGINWMAFLWSKGDNGILADEMGLGKTVQTVAFISWLIF ARRQNGPHIIVVPLSTMPAWLDTFEKWAPDLNCICYMGNQKSRDTIREYEFYTNPRAKGK KTMKFNVLLTTYEYILKDRAELGSIKWQFMAVDEAHRLKNAESSLYESLNSFKVANRMLI TGTPLQNNIKELAALVNFLMPGRFTIDQEIDFENQDEEQEEYIHDLHRRIQPFILRRLKK DVEKSLPSKTERILRVELSDVQTEYYKNILTKNYSALTAGAKGGHFSLLNIMNELKKASN HPYLFDNAEERVLQKFGDGKMTRENVLRGLIMSSGKMVLLDQLLTRLKKDGHRVLIFSQM VRMLDILGDYLSIKGINFQRLDGTVPSAQRRISIDHFNSPDSNDFVFLLSTRAGGLGINL MTADTVVIFDSDWNPQADLQAMARAHRIGQKNHVMVYRLVSKDTVEEEVLERARKKMILE YAIISLGVTDGNKYTKKNEPNAGELSAILKFGAGNMFTATDNQKKLEDLNLDDVLNHAED HVTTPDLGESHLGGEEFLKQFEVTDYKADIDWDDIIPEEELKKLQDEEQKRKDEEYVKEQ LEMMNRRDNALKKIKNSVNGDGTAANSDSDDDSTSRSSRRRARANDMDSIGESEVRALYK AILKFGNLKEILDELIADGTLPVKSFEKYGETYDEMMEAAKDCVHEEEKNRKEILEKLEK HATAYRAKLKSGEIKAENQPKDNPLTRLSLKKREKKAVLFNFKGVKSLNAESLLSRVEDL KYLKNLINSNYKDDPLKFSLGNNTPKPVQNWSSNWTKEEDEKLLIGVFKYGYGSWTQIRD DPFLGITDKIFLNEVHNPVAKKSASSSDTTPTPSKKGKGITGSSKKVPGAIHLGRRVDYL LSFLRGGLNTKSPSADIGSKKLPTGPSKKRQRKPANHSKSMTPEITSSEPANGPPSKRMK ALPKGPAALINNTRLSPNSPTPPLKSKVSRDNGTRQSSNPSSGSAHEKEYDSMDEEDCRH TMSAIRTSLKRLRRGGKSLDRKEWAKILKTELTTIGNHIESQKGSSRKASPEKYRKHLWS YSANFWPADVKSTKLMAMYDKITESQKK
experiment.sample.molecule[0].mw116.922
experiment.sample.molecule[0].total_mw116.922
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.buffer.name50mM Hepes 150mM NaCl
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.nameN-terminal and chromo-ATPase domains of chromo domain-containing protein 1 (Chd1: 1-1010)
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].addressDundee, UK
experiment.contributor[0].affiliation[0].full_nameUniversity of Dundee
experiment.contributor[0].affiliation[0].webpagehttps://www.dundee.ac.uk/
experiment.contributor[0].contributor_nameRamasubramanian
experiment.contributor[0].contributor_surnameSundaramoorthy
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2008-11-30
experiment.storage_temperature10.0
experiment.cell_temperature10.0
experiment.exposure_time120.0
experiment.number_of_framesnull
experiment.wavelength0.154
experiment.sample_detector_distance5.0
experiment.concentration_min0.6
experiment.concentration_max9.8
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.073
experiment.s_max4.945
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].symmetryC1
fits[0].models[0].comment
fits[0].models[0].user184
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fits[0].chi_square_value5.4
fits[0].p_value0.0
fits[0].fit_residual_plotSASDBY7_fit1_fitresiduals_img.png
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fits[0].fit_lognull
fits[0].software_version
fits[0].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionnull
i0_calibration_standardnull
descriptionThe protein fragment 1-1010 encompassing the N-terminal and chromo-ATPase domains of Saccharomyces cerevisiae Chd1.
experiment_descriptionSynchrotron SAXS data from solutions of the N-terminal-chromo-ATPase domains of chromo domain-containing protein 1 (Chd1: 1-1010) in 50mM HEPES, 150mM NaCl, pH 7.5 were collected at the X33 beam line on the DORIS III storage ring (Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 5 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsin θ/λ and 2θ is the scattering angle). Solute concentrations ranging between 0.6 and 9.8 mg/ml were measured at 10°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the different curves were scaled for protein concentration. The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.
tags[0]X33
intensity_unitnull
experimental_mw120.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i01.22
pddf_i0_error0.001
guinier_i01.36
guinier_i0_error0.0035
pddf_rg4.07
pddf_rg_error0.002
guinier_rg4.53
guinier_rg_error0.01
pddf_dmax12.0
pddf_dmax_errornull
porod_volume228.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first7
guinier_point_last94
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDBY7_datloglog_img.png
symmetrynull
last_modified2023-05-25T11:22:08.798758+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDBY7
statussuccess
started_at2026-08-11T15:42:27.282121+00:00
finished_at2026-08-11T15:42:39.613751+00:00
source_last_modified2023-05-25T11:22:08.798758+02:00
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View the complete summary.json source
{
  "code": "SASDBY7",
  "status": "Published",
  "type_of_curve": "Extrapolated to infinite dilution",
  "angular_unit": "1/nm",
  "project": {
    "title": "Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes.",
    "publication": {
      "title": "Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes.",
      "author_list": "Sundaramoorthy R, Hughes AL, Singh V, Wiechens N, Ryan DP, El-Mkami H, Petoukhov M, Svergun DI, Treutlein B, Quack S, Fischer M, Michaelis J, Böttcher B, Norman DG, Owen-Hughes T",
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View the complete manifest.json source
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