SASDCQ5

SAXS on intact Doryteuthis squid lens 100% layer

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2025-07-02T09:29:22.089567+02:00
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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · SAXS on intact Doryteuthis squid lens 100% layer

Concentration— – — Buffer / pHTissue fluid / 7.0
Experimental temperature10.0 Facility / beamlineNational Synchrotron Light Source (NSLS) / X9A
Wavelength0.103318 nmExposure60.0 s × 1

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
S-crystallin, Q25367_DOROP
View sequence
MPTYTLYYFNGRGRAEVLRMMFAAANVKYMDKRFEFNEWDKYRKDMPSMCVPVLEMDGGNKMPETMAIPRYLAREFGFYGKSNMDMMRCDYIADCFYEIMHDYMRYFHEKNGRFRSSMEGSGNGMNSPTGASGDMNSNSNFDTYLQWRFMNTCNRVLPFLERTLEMQNGGKAFFMGDQMMWCDMMCHCALEGPFMENQSMLSKHPKLMALRTRIASHPKISGYLKSRSNTNW
proteinDoryteuthis pealeiiQ253671–232dimerMolecule count 227.289 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11993[2]0.004–1.0 1/ANo uncertainty columnMissing 19930sasbdb/entries/q5/sasdcq5/source/SASDCQ5.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
mwExperimental50.0—kDa
rgP(r)2.4—Å

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 nameTissue fluidBuffer concentration—
pH7.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2014-07-17Storage / measurement temperature10.0 / 10.0
Exposure time60.0Frames1
Wavelength0.103318Sample-to-detector distance—
SourceX-ray synchrotronDetectorPilatus 300K
Facility / beamlineNational Synchrotron Light Source (NSLS) / X9A · Brookhaven, NY, USA
q range0.04 – 10.0Sample volume / flow rate— / —

Original SASBDB Plots

Experimental I(q)
Experimental I(q)
Experimental I(q), log-log
Experimental I(q), log-log
Kratky plot
Kratky 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:156 field values
Field pathRaw value
codeSASDCQ5
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleEye patches: Protein assembly of index-gradient squid lenses.
project.publication.titleEye patches: Protein assembly of index-gradient squid lenses.
project.publication.author_listCai J, Townsend JP, Dodson TC, Heiney PA, Sweeney AM
project.publication.journalScience
project.publication.doi10.1126/science.aal2674
project.publication.pmid28798124
project.publication.published_date2017 Aug 11
project.statusreleased
project.submitted_date2017-06-29
project.released_date2017-08-18
pddf_datanull
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experiment.instrument.detector.resolutionnull
experiment.instrument.nameNational Synchrotron Light Source (NSLS)
experiment.instrument.cityBrookhaven, NY
experiment.instrument.countryUSA
experiment.instrument.beamline_nameX9A
experiment.instrument.beam_geometry
experiment.instrument.type_of_sourceX-ray synchrotron
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experiment.sample.molecule[0].long_nameS-crystallin, Q25367_DOROP
experiment.sample.molecule[0].short_nameS-crystallin, Q25367
experiment.sample.molecule[0].sequenceMPTYTLYYFNGRGRAEVLRMMFAAANVKYMDKRFEFNEWDKYRKDMPSMCVPVLEMDGGN KMPETMAIPRYLAREFGFYGKSNMDMMRCDYIADCFYEIMHDYMRYFHEKNGRFRSSMEG SGNGMNSPTGASGDMNSNSNFDTYLQWRFMNTCNRVLPFLERTLEMQNGGKAFFMGDQMM WCDMMCHCALEGPFMENQSMLSKHPKLMALRTRIASHPKISGYLKSRSNTNW
experiment.sample.molecule[0].organismDoryteuthis pealeii
experiment.sample.molecule[0].uniprot_codeQ25367
experiment.sample.molecule[0].uniprot_range_first1
experiment.sample.molecule[0].uniprot_range_last232
experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMPTYTLYYFNGRGRAEVLRMMFAAANVKYMDKRFEFNEWDKYRKDMPSMCVPVLEMDGGN KMPETMAIPRYLAREFGFYGKSNMDMMRCDYIADCFYEIMHDYMRYFHEKNGRFRSSMEG SGNGMNSPTGASGDMNSNSNFDTYLQWRFMNTCNRVLPFLERTLEMQNGGKAFFMGDQMM WCDMMCHCALEGPFMENQSMLSKHPKLMALRTRIASHPKISGYLKSRSNTNW
experiment.sample.molecule[0].mw27.289
experiment.sample.molecule[0].total_mw54.578
experiment.sample.molecule[0].number_molecules2
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experiment.sample.buffer.pkanull
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experiment.sample.purity_methodnull
experiment.sample.nameSAXS on intact Doryteuthis squid lens 100% layer
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_namePenn
experiment.contributor[0].affiliation[0].addressPhiladelphia, PA, United States
experiment.contributor[0].affiliation[0].full_nameUniversity of Pennsylvania
experiment.contributor[0].affiliation[0].webpagehttp://www.upenn.edu/
experiment.contributor[0].contributor_nameJing
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experiment.concentration_methodnull
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experiment.date2014-07-17
experiment.storage_temperature10.0
experiment.cell_temperature10.0
experiment.exposure_time60.0
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experiment_descriptionThis dataset is SAXS characterization of the peripheral region (tissue from radial positions of 100%–80% of the total lens radius) of the intact Doryteuthis squid eye lens tissue. The lens contains about 40 unique S-crystallins isoforms that vary in molecular weight due to length variation in a disordered region encoded in the central exon of the coding sequence such that loops form protruding from the folded protein. S-crystallins are dimeric and globular, such that each dimer has two of these disordered loops, which form linking structures between particles in the system. Because the proteins link to form extended materials, even at very low concentration, the parameter Rg does not apply here. Similarly, because this is a measurement of intact biological tissue, there is no experimental buffer per se to subtract, and accordingly, raw data without buffer subtraction are reported here. The pair-distance distribution function (p(r)) was calculated based on unsubtracted data (refer to the full entry zip archive for the p(r) profile). The full set of sequences describing the protein polydispersity in this system is available at GenBank BioProject PRJNA386124. Synchrotron SAXS data were collected on the X9A beam line of the National Synchrotron Light Source (NSLS; Brookhaven, NY, USA) using a 20Hz Pilatus 300K detector at a wavelength of λ = 0.103318 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). The sample measurement (1 x 60 s exposure) was performed at at 10°C.
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intensities_log_log_plotSASDCQ5_datloglog_img.png
symmetrynull
last_modified2025-07-02T09:29:22.089567+02:00
bragg_peak[]
manifest.json:33 field values
Field pathRaw value
codeSASDCQ5
statussuccess
started_at2026-08-11T14:53:11.088466+00:00
finished_at2026-08-11T14:53:17.362686+00:00
source_last_modified2025-07-02T09:29:22.089567+02:00
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View the complete summary.json source
{
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  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Eye patches: Protein assembly of index-gradient squid lenses.",
    "publication": {
      "title": "Eye patches: Protein assembly of index-gradient squid lenses.",
      "author_list": "Cai J, Townsend JP, Dodson TC, Heiney PA, Sweeney AM",
      "journal": "Science",
      "doi": "10.1126/science.aal2674",
      "pmid": "28798124",
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      "fit_data": "https://www.sasbdb.org/media/fitting_files/SASDCQ5_fit1.fir",
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  "description": null,
  "experiment_description": "This dataset is SAXS characterization of the peripheral region (tissue from radial positions of 100%–80% of the total lens radius) of the intact Doryteuthis squid eye lens tissue. The lens contains about 40 unique S-crystallins isoforms that vary in molecular weight due to length variation in a disordered region encoded in the central exon of the coding sequence such that loops form protruding from the folded protein. S-crystallins are dimeric and globular, such that each dimer has two of these disordered loops, which form linking structures between particles in the system. Because the proteins link to form extended materials, even at very low concentration, the parameter Rg does not apply here. Similarly, because this is a measurement of intact biological tissue, there is no experimental buffer per se to subtract, and accordingly, raw data without buffer subtraction are reported here. The pair-distance distribution function (p(r)) was calculated based on unsubtracted data (refer to the full entry zip archive for the p(r) profile). The full set of sequences describing the protein polydispersity in this system is available at GenBank BioProject PRJNA386124. Synchrotron SAXS data were collected on the X9A beam line of the National Synchrotron Light Source (NSLS; Brookhaven, NY, USA) using a 20Hz Pilatus 300K detector at a wavelength of λ = 0.103318 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). The sample measurement (1 x 60 s exposure) was performed at at 10°C.",
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  "last_modified": "2025-07-02T09:29:22.089567+02:00",
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}
View the complete manifest.json source
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