SASDX77

Palladin Ig3-Ig4 tandem domain with linker swapped for the shorter Ig4-Ig5 Linnker

Data type: SASBDB experimental data Status: Published Curve type: Merged Last updated: 2026-02-19T15:23:41.262536+01:00

Synchrotron SAXS data from solutions of the Ig-like C2-type 3 and Ig-like C2-type 4 domains (Ig34) of palladin where the wildtype linker region has been replaced by shorter linker found between Ig4 and Ig5 domains in 20 mM HEPES pH 7.4, 1 mM DTT, 100 mM NaCl were collected on the BL4-2 beam line at the Stanford Synchrotron Radiation Lightsource (SSR; Menlo Park, CA, USA) using a Rayonix MX225-HE detector at a sample-detector distance of 1.2 m and at a wavelength of λ = 0.113 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.5 and 10.0 mg/ml were measured at 20°C. 12 successive 1 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.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Palladin Ig3-Ig4 tandem domain with linker swapped for the shorter Ig4-Ig5 Linnker

Concentration— – — Buffer / pHHEPES / 7.4
Experimental temperature— Facility / beamlineStanford Synchrotron Radiation Lightsource (SSRL) / BL4-2
Wavelength— nmExposure— s × —

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Palladin Ig3-45Linker_Ig4
View sequence
>PALLADINIG3-45L-IG4SNANATAPFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANPQGRVSCTGRLMVQAKEAHKAPVFMEKLQNTGVADGYPVRLECRVSGVPPPQIFWKKENESLTHSTERVSMHQDNHGYICLLIQGATKEDAGWYTVSAKNEAGIVSCTARLDVY
proteinMus musculusQ9ET541022–1257monomerMolecule count 122.3 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1950[3]0.0103666–0.7382874 1/AHas uncertainty columnMissing 00sasbdb/entries/77/sasdx77/source/SASDX77.dat
▼

2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)10.42—Å
i0Guinier0.00785779—arbitrary
i0P(r)0.007908—arbitrary
mwExperimental28.9—kDa
mwGuinier I(0)28.9—kDa
mwPorod34.6—kDa
porod_volumePorod26.8—ų
rgGuinier2.8860.165Å
rgP(r)3.0—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 nameHEPESBuffer concentration—
pH7.4Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2023-08-29Storage / measurement temperature— / —
Exposure time—Frames—
Wavelength—Sample-to-detector distance—
SourceX-ray synchrotronDetectorRayonix MX225-HE
Facility / beamlineStanford Synchrotron Radiation Lightsource (SSRL) / BL4-2 · Menlo Park, CA, USA
q range0.104 – 7.383Sample 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:182 field values
Field pathRaw value
codeSASDX77
statusPublished
type_of_curveMerged
angular_unit1/A
project.titleThe role of linker length and composition in actin binding and bundling by palladin.
project.publication.titleThe role of linker length and composition in actin binding and bundling by palladin.
project.publication.author_listSargent RA, Bradford CW, Hughes LM, Ta NH, Limpiado MJ, Vattepu R, Beck MR
project.publication.journalBiochem J
project.publication.doi10.1042/BCJ20250187
project.publication.pmid41553766
project.publication.published_date2026 Mar 4
project.statusreleased
project.submitted_date2025-08-01
project.released_date2026-02-19
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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_namePalladin Ig3-45Linker_Ig4
experiment.sample.molecule[0].short_namePalladin Ig3-45L-Ig4
experiment.sample.molecule[0].sequence>palladin Ig3-45L-Ig4 SNANATAPFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANPQGRVSCTGRLMVQAKEAHKAPVFMEKLQNTGVADGYPVRLECRVSGVPPPQIFWKKENESLTHSTERVSMHQDNHGYICLLIQGATKEDAGWYTVSAKNEAGIVSCTARLDVY
experiment.sample.molecule[0].organismMus musculus
experiment.sample.molecule[0].uniprot_codeQ9ET54
experiment.sample.molecule[0].uniprot_range_first1022
experiment.sample.molecule[0].uniprot_range_last1257
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMSETSSHDSFYDSLSDVQEEGKSADFFPGLSAFLSQEEINKSLDLARRAIDSSETEDFDS EKEISQIFSKSPISLCETPSHEEPKSGKQTSSERPQDSRRAPVQPLTGDQAERITSPGSK RKPGVSPLLASPSYIRSLRKAEKRGAKNPNPSSKPKTAQQSKAGPQSQLCDKAASFIEEL TSIFREAAKPRNRSPNGESSSPDSGYLSPKNQPSALMSASASQSPTADQLDQLEMDAEVK QAQGSLCYQAHQASEETLPLAHIPHPQPQKARHLPTAPRFIQKLRSQEVAEGSRVYLECR VTGNPTPRVRWFCEGKELYNSPDVQIHCESGELHTLVIAEAFEDDTGRYTCLATNPSGSD STSAEVFIEGASSTDSDSESLSFISKAGAMPQAQKKTTSVSLTIGSSAPKTGVTTAVIQP LSVPVQQAHSATSYLCRPDGTTMGCLLPVFTKELQNTAASEGQVVVLECRVRGAPPLQVQ WFRQGSEIQDSPDFRILQKKPRSTAEPEEICTLVIAESFPEDAGIFTCSATNDYGSVTST AQLVITSANNENCSYDSTGEPNSDHFQHFPPPPPILETGSYELASQKPSEIQQVNSPNLG FSMAALQMQFNTAERETNGVHPSHGVNGLINGKAYGNKSPPTPTALLSPTKEPPPLLAKP KLDPLKLQQLQNQVRLEQEACAWPPAPPGVPCNSSSSGSSAPPSPPFPPPPPAFPELAAC ASPVPSEPMSALASRATAMQSSGSFNYARPKQFIAAQNLGPASGLPTPTSSPSSSSLPSP LSPTPRPFGRAPGPPFVEPEAMWGPSSPSPPPPPPPVFSPSAAYPVPDVFPLPPPPPPLP SSTSHCASPARFGPSQTPAAFLSALLPSQPPPVAVNALGLPKGVTPAGFPKKSSRTARIA SDEEIQGTKDAVIQDLERKLRFKEDLLNNGQPRLTYEERMARRLLGADSANVFNIQEPEE TAANQDAGAPRASVGGPLDGQKEYKVSSCEQRLISEIEYRLERSPVDESGDEVQDPDVPV ENATAPFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRDLD GTCSLHTTASTLDDDGNYTIMAANPQGRVSCTGRLMVQAVNQRGRSPRSPSGHPHARRPR SRSRDSGDENEPIQERFFRPHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPI RPDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIATNRAGQNSFNLELVVAAKEAHKAPV FMEKLQNTGVADGYPVRLECRVSGVPPPQIFWKKENESLTHSTERVSMHQDNHGYICLLI QGATKEDAGWYTVSAKNEAGIVSCTARLDVYTQWHQQPQTTKPKKVRPSASRYAALSDQG LDIKAAFQPEASPSHLTLNSGLVESEDL
experiment.sample.molecule[0].mw22.3
experiment.sample.molecule[0].total_mw22.3
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_descriptionTandem immunoglobulin domains (Ig) of palladin involved in actin binding and bundling where the native 41-residue linker between the Ig3 and Ig4 domain has been relplaced with the much shorter 7-residue linker that naturally connects Ig4 to Ig5 in full-length palladin.
experiment.sample.buffer.nameHEPES
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.4
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.namePalladin Ig3-Ig4 tandem domain with linker swapped for the shorter Ig4-Ig5 Linnker
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_nameWichita State University
experiment.contributor[0].affiliation[0].webpagenull
experiment.contributor[0].contributor_nameMoriah
experiment.contributor[0].contributor_surnameBeck
experiment.contributor[0].orcidhttps://orcid.org/0000-0003-1004-7147
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2023-08-29
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
experiment.sample_volumenull
experiment.flow_ratenull
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experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].p_value0.2134
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fits[0].description
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pddf_software_versionnull
i0_calibration_standardnull
descriptionSynchrotron SAXS data from solutions of the Ig-like C2-type 3 and Ig-like C2-type 4 domains (Ig34) of palladin where the wildtype linker region has been replaced by shorter linker found between Ig4 and Ig5 domains in 20 mM HEPES pH 7.4, 1 mM DTT, 100 mM NaCl were collected on the BL4-2 beam line at the Stanford Synchrotron Radiation Lightsource (SSR; Menlo Park, CA, USA) using a Rayonix MX225-HE detector at a sample-detector distance of 1.2 m and at a wavelength of λ = 0.113 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.5 and 10.0 mg/ml were measured at 20°C. 12 successive 1 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.
experiment_descriptionnull
tags[]
intensity_unitarbitrary
experimental_mw28.9
experimental_mw_errornull
guinier_i0_mw28.9
guinier_i0_mw_errornull
porod_mw34.6
porod_mw_errornull
pddf_i00.007908
pddf_i0_errornull
guinier_i00.00785779
guinier_i0_errornull
pddf_rg3.0
pddf_rg_errornull
guinier_rg2.886
guinier_rg_error0.165
pddf_dmax10.42
pddf_dmax_errornull
porod_volume26.8
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first2
guinier_point_last42
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDX77_datloglog_img.png
symmetrynull
last_modified2026-02-19T15:23:41.262536+01:00
bragg_peak[]
manifest.json:34 field values
Field pathRaw value
codeSASDX77
statussuccess
started_at2026-08-11T15:23:52.559734+00:00
finished_at2026-08-11T15:24:00.412613+00:00
source_last_modified2026-02-19T15:23:41.262536+01:00
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View the complete summary.json source
{
  "code": "SASDX77",
  "status": "Published",
  "type_of_curve": "Merged",
  "angular_unit": "1/A",
  "project": {
    "title": "The role of linker length and composition in actin binding and bundling by palladin.",
    "publication": {
      "title": "The role of linker length and composition in actin binding and bundling by palladin.",
      "author_list": "Sargent RA, Bradford CW, Hughes LM, Ta NH, Limpiado MJ, Vattepu R, Beck MR",
      "journal": "Biochem J",
      "doi": "10.1042/BCJ20250187",
      "pmid": "41553766",
      "published_date": "2026 Mar 4"
    },
    "status": "released",
    "submitted_date": "2025-08-01",
    "released_date": "2026-02-19"
  },
  "pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDX77.out",
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        }
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    "contributor": [
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        "affiliation": [
          {
            "short_name": null,
            "address": null,
            "full_name": "Wichita State University",
            "webpage": null
          }
        ],
        "contributor_name": "Moriah",
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        "orcid": "https://orcid.org/0000-0003-1004-7147"
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    "concentration_method": null,
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    "date": "2023-08-29",
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  "last_modified": "2026-02-19T15:23:41.262536+01:00",
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}
View the complete manifest.json source
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