SASDVQ5

HTT1 peptide

Data type: SASBDB experimental data Status: Published Curve type: Merged Last updated: 2024-08-18T16:49:40.970362+02:00

The sodium phosphate buffer solution contains 480 μL of 10 mM PB, pH 7.4, 16.5 μL of 100 mM NaOH, and 10 μL of 1% trifluoroacetic acid (TFA).

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · HTT1 peptide

Concentration4.0 – 8.0 Buffer / pHSodium phosphate buffer / 7.4
Experimental temperature10.0 Facility / beamlineNSRRC / TPS13A
Wavelength0.08265 nmExposure2.0 s × 3

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
HTT1
View sequence
MATPEKPMKAFESPKSFLQQLQQQLQQLQQQYK
proteinsynthetic construct——–—dimerMolecule count 23.952 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1529[3]0.01157–1.0014 1/AHas uncertainty columnMissing 00sasbdb/entries/q5/sasdvq5/source/SASDVQ5.dat
▼

2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)7.0—Å
i0Guinier0.025966—1/cm
mwExperimental19.0—kDa
porod_volumePorod18.0—ų
rgGuinier1.90.134Å

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.

▶

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 nameSodium phosphate bufferBuffer concentration—
pH7.4Additives—
Buffer description(PB) solution (containing 480 μL of 10 mM PB, pH 7.4, 16.5 μL of 100 mM NaOH, and 10 μL of 1% TFA)
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2021-02-03Storage / measurement temperature10.0 / 10.0
Exposure time2.0Frames3
Wavelength0.08265Sample-to-detector distance2.5
SourceX-ray synchrotronDetectorEiger X 1M & 9M
Facility / beamlineNSRRC / TPS13A · Hsinchu, Taiwan
q range0.116 – 10.014Sample volume / flow rate70.0 / 0.35

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

Downloadable Files

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pddfsasbdb/entries/q5/sasdvq5/source/SASDVQ5.outnot_listed——DownloadView source file
sascifsasbdb/entries/q5/sasdvq5/source/SASDVQ5.sascifnot_available——DownloadView source fileSource site
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full_entry_zip:source record and ZIP contents (1 items)
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sascif:source record
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summary:source record
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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
codeSASDVQ5
statusPublished
type_of_curveMerged
angular_unit1/A
project.titleBinding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation.
project.publication.titleBinding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation.
project.publication.author_listLin TC, Shih O, Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
project.publication.journalIUCrJ
project.publication.doi10.1107/S2052252524006341
project.publication.pmid39120045
project.publication.published_date2024 Sep 1
project.statusreleased
project.submitted_date2024-08-01
project.released_date2024-08-07
pddf_datanull
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pddf_plotnull
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experiment.instrument.detector.typenull
experiment.instrument.detector.nameEiger X 1M & 9M
experiment.instrument.detector.resolution0.001
experiment.instrument.nameNSRRC
experiment.instrument.cityHsinchu
experiment.instrument.countryTaiwan
experiment.instrument.beamline_nameTPS13A
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_nameHTT1
experiment.sample.molecule[0].short_namenull
experiment.sample.molecule[0].sequenceMATPEKPMKAFESPKSFLQQLQQQLQQLQQQYK
experiment.sample.molecule[0].organismsynthetic construct
experiment.sample.molecule[0].uniprot_codenull
experiment.sample.molecule[0].uniprot_range_firstnull
experiment.sample.molecule[0].uniprot_range_lastnull
experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequence
experiment.sample.molecule[0].mw3.952
experiment.sample.molecule[0].total_mw7.904
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_description
experiment.sample.buffer.nameSodium phosphate buffer
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.comment(PB) solution (containing 480 μL of 10 mM PB, pH 7.4, 16.5 μL of 100 mM NaOH, and 10 μL of 1% TFA)
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.4
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameHTT1 peptide
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].addressHsinchu City, Taiwan
experiment.contributor[0].affiliation[0].full_nameNational Synchrotron Radiation Research Center
experiment.contributor[0].affiliation[0].webpagehttps://www.nsrrc.org.tw/
experiment.contributor[0].contributor_nameOrion
experiment.contributor[0].contributor_surnameShih
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2021-02-03
experiment.storage_temperature10.0
experiment.cell_temperature10.0
experiment.exposure_time2.0
experiment.number_of_frames3
experiment.wavelength0.08265
experiment.sample_detector_distance2.5
experiment.concentration_min4.0
experiment.concentration_max8.0
experiment.sample_volume70.0
experiment.flow_rate0.35
experiment.s_min0.116
experiment.s_max10.014
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwarenull
pddf_software_versionnull
i0_calibration_standardnull
descriptionThe sodium phosphate buffer solution contains 480 μL of 10 mM PB, pH 7.4, 16.5 μL of 100 mM NaOH, and 10 μL of 1% trifluoroacetic acid (TFA).
experiment_descriptionSynchrotron SAXS data from solutions of HTT1 peptide in sodium phosphate buffer, pH 7.4 were collected on the TPS13A beam line at the NSRRC (Hsinchu, Taiwan) using a Eiger X 1M & 9M detector at a sample-detector distance of 2.5 m and at a wavelength of λ = 0.08265 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 4 and 8 mg/ml were measured at 10°C. Three successive 2 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.
tags[]
intensity_unit1/cm
experimental_mw19.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i0null
pddf_i0_errornull
guinier_i00.025966
guinier_i0_errornull
pddf_rgnull
pddf_rg_errornull
guinier_rg1.9
guinier_rg_error0.134
pddf_dmax7.0
pddf_dmax_errornull
porod_volume18.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first50
guinier_point_last106
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDVQ5_datloglog_img.png
symmetrynull
last_modified2024-08-18T16:49:40.970362+02:00
bragg_peak[]
manifest.json:31 field values
Field pathRaw value
codeSASDVQ5
statussuccess
started_at2026-08-11T14:53:31.763526+00:00
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View the complete summary.json source
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    "title": "Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation.",
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      "author_list": "Lin TC, Shih O, Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US",
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View the complete manifest.json source
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