SASDA77

Surface Protein G (SasG) EG5 repeat protein G51-G56

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2023-06-21T07:56:39.492710+02:00

SAXS was used to determine whether the EG5 repeat forms an extended rod-like structure in solution.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Surface Protein G (SasG) EG5 repeat protein G51-G56

Concentration— – 4.0 Buffer / pH20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl / 7.5
Experimental temperature10.0 Facility / beamlinePETRA III / EMBL P12
Wavelength0.12 nmExposure0.05 s × 20

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Surface protein G
View sequence
GPAMAPKTITELEKKVEEIPFKKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGVIISKGEPKEEITKDPINELTEYGPETIAPGHRDEFDPKLPTGEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFEKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGEIISKGESKEEITKDPINELTEYGPETITPGHRDEFDPKLPTGEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFEKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGVIISKGEPKEEITKDPINELTEYGPETITPGHRDEFDPKLPTGEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFKKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGEIISKGESKEEITKDPINELTEYGPETITPGHRDEFDPKLPTGEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFEKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGEIISKGESKEEITKDPINELTEYGPETITPGHRDEFDPKLPTGEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFKKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGEIISKGESKEEITKDPINELTEYGPETWSHPQFEK
proteinStaphylococcus aureusQ2G2B2419–1141monomerMolecule count 180.922 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11687[3]0.0475023–4.48844 1/nmHas uncertainty columnMissing 08sasbdb/entries/77/sasda77/source/SASDA77.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)57.0—nm
i0Guinier10488.6——
i0P(r)13550.0——
mwExperimental69.7—kDa
mwGuinier I(0)69.7—kDa
mwPorod74.0—kDa
porod_volumePorod89.2—nm³
rgGuinier14.1—nm
rgP(r)15.48—nm

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 200 mM NaCl 1 mM EDTA 20 mM Tris.ClBuffer concentration20.0 mM
pH7.5Additives200 mM NaCl, 1 mM EDTA, 20 mM Tris.Cl
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2013-11-12Storage / measurement temperature10.0 / 10.0
Exposure time0.05Frames20
Wavelength0.12Sample-to-detector distance3.1
SourceX-ray synchrotronDetectorPilatus 2M
Facility / beamlinePETRA III / EMBL P12 · DESY; Hamburg, Germany
q range0.048 – 4.488Sample 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 (6 items)
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sascif: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:179 field values
Field pathRaw value
codeSASDA77
statusPublished
type_of_curveSingle concentration
angular_unit1/nm
project.titleCooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein.
project.publication.titleCooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein.
project.publication.author_listGruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J
project.publication.journalNat Commun
project.publication.doi10.1038/ncomms8271
project.publication.pmid26027519
project.publication.published_date2015 Jun 1
project.statusreleased
project.submitted_date2014-11-27
project.released_date2015-07-07
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDA77.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDA77.dat
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sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDA77.sascif
experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus 2M
experiment.instrument.detector.resolutionnull
experiment.instrument.namePETRA III
experiment.instrument.cityDESY; Hamburg
experiment.instrument.countryGermany
experiment.instrument.beamline_nameEMBL P12
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_nameSurface protein G
experiment.sample.molecule[0].short_nameSasG
experiment.sample.molecule[0].sequenceGPAMAPKTITELEK KVEEIPFKKE RKFNPDLAPG TEKVTREGQK GEKTITTPTL KNPLTGVIIS KGEPKEEITK DPINELTEYG PETIAPGHRD EFDPKLPTGE KEEVPGKPGI KNPETGDVVR PPVDSVTKYG PVKGDSIVEK EEIPFEKERK FNPDLAPGTE KVTREGQKGE KTITTPTLKN PLTGEIISKG ESKEEITKDP INELTEYGPE TITPGHRDEF DPKLPTGEKE EVPGKPGIKN PETGDVVRPP VDSVTKYGPV KGDSIVEKEE IPFEKERKFN PDLAPGTEKV TREGQKGEKT ITTPTLKNPL TGVIISKGEP KEEITKDPIN ELTEYGPETI TPGHRDEFDP KLPTGEKEEV PGKPGIKNPE TGDVVRPPVD SVTKYGPVKG DSIVEKEEIP FKKERKFNPD LAPGTEKVTR EGQKGEKTIT TPTLKNPLTG EIISKGESKE EITKDPINEL TEYGPETITP GHRDEFDPKL PTGEKEEVPG KPGIKNPETG DVVRPPVDSV TKYGPVKGDS IVEKEEIPFE KERKFNPDLA PGTEKVTREG QKGEKTITTP TLKNPLTGEI ISKGESKEEI TKDPINELTE YGPETITPGH RDEFDPKLPT GEKEEVPGKP GIKNPETGDV VRPPVDSVTK YGPVKGDSIV EKEEIPFKKE RKFNPDLAPG TEKVTREGQK GEKTITTPTL KNPLTGEIIS KGESKEEITK DPINELTEYG PETWSHPQFEK
experiment.sample.molecule[0].organismStaphylococcus aureus
experiment.sample.molecule[0].uniprot_codeQ2G2B2
experiment.sample.molecule[0].uniprot_range_first419
experiment.sample.molecule[0].uniprot_range_last1141
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMRDKKGPVNKRVDFLSNKLNKYSIRKFTVGTASILIGSLMYLGTQQEAEAAENNIENPTT LKDNVQSKEVKIEEVTNKDTAPQGVEAKSEVTSNKDTIEHEPSVKAEDISKKEDTPKEVA DVAEVQPKSSVTHNAETPKVRKARSVDEGSFDITRDSKNVVESTPITIQGKEHFEGYGSV DIQKKPTDLGVSEVTRFNVGNESNGLIGALQLKNKIDFSKDFNFKVRVANNHQSNTTGAD GWGFLFSKGNAEEYLTNGGILGDKGLVNSGGFKIDTGYIYTSSMDKTEKQAGQGYRGYGA FVKNDSSGNSQMVGENIDKSKTNFLNYADNSTNTSDGKFHGQRLNDVILTYVASTGKMRA EYAGKTWETSITDLGLSKNQAYNFLITSSQRWGLNQGINANGWMRTDLKGSEFTFTPEAP KTITELEKKVEEIPFKKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGVIISKG EPKEEITKDPINELTEYGPETIAPGHRDEFDPKLPTGEKEEVPGKPGIKNPETGDVVRPP VDSVTKYGPVKGDSIVEKEEIPFEKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPL TGEIISKGESKEEITKDPINELTEYGPETITPGHRDEFDPKLPTGEKEEVPGKPGIKNPE TGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFEKERKFNPDLAPGTEKVTREGQKGEKTIT TPTLKNPLTGVIISKGEPKEEITKDPINELTEYGPETITPGHRDEFDPKLPTGEKEEVPG KPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFKKERKFNPDLAPGTEKVTREG QKGEKTITTPTLKNPLTGEIISKGESKEEITKDPINELTEYGPETITPGHRDEFDPKLPT GEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFEKERKFNPDLAPG TEKVTREGQKGEKTITTPTLKNPLTGEIISKGESKEEITKDPINELTEYGPETITPGHRD EFDPKLPTGEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFKKERK FNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGEIISKGESKEEITKDPINELTEYGPE TITPGHRDEFDPKLPTGEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEE IPFEKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGEIISKGESKEEITKDPIN ELTEYGPETITPGHRDEFDPKLPTGEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKG DSIVEKEEIPFEKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGEIISKGESKE EITKDPVNELTEFGGEKIPQGHKDIFDPNLPTDQTEKVPGKPGIKNPDTGKVIEEPVDDV IKHGPKTGTPETKTVEIPFETKREFNPKLQPGEERVKQEGQPGSKTITTPITVNPLTGEK VGEGQPTEEITKQPVDKIVEFGGEKPKDPKGPENPEKPSRPTHPSGPVNPNNPGLSKDRA KPNGPVHSMDKNDKVKKSKIAKESVANQEKKRAELPKTGLESTQKGLIFSSIIGIAGLML LARRRKN
experiment.sample.molecule[0].mw80.922
experiment.sample.molecule[0].total_mw80.922
experiment.sample.molecule[0].number_molecules1
experiment.sample.molecule[0].complex_statenull
experiment.sample.molecule[0].deuterationnull
experiment.sample.molecule[0].molecule_sourcebiological
experiment.sample.molecule[0].molecule_descriptionnull
experiment.sample.buffer.name20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl
experiment.sample.buffer.concentration_unitmM
experiment.sample.buffer.commentnull
experiment.sample.buffer.additive200 mM NaCl, 1 mM EDTA, 20 mM Tris.Cl
experiment.sample.buffer.concentration20.0
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameSurface Protein G (SasG) EG5 repeat protein G51-G56
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_nameFiona
experiment.contributor[0].contributor_surnameWhelan
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2013-11-12
experiment.storage_temperature10.0
experiment.cell_temperature10.0
experiment.exposure_time0.05
experiment.number_of_frames20
experiment.wavelength0.12
experiment.sample_detector_distance3.1
experiment.concentration_minnull
experiment.concentration_max4.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.048
experiment.s_max4.488
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[1].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionnull
i0_calibration_standardnull
descriptionSAXS was used to determine whether the EG5 repeat forms an extended rod-like structure in solution.
experiment_descriptionnull
tags[]
intensity_unitnull
experimental_mw69.7
experimental_mw_errornull
guinier_i0_mw69.7
guinier_i0_mw_errornull
porod_mw74.0
porod_mw_errornull
pddf_i013550.0
pddf_i0_errornull
guinier_i010488.6
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pddf_rg_errornull
guinier_rg14.1
guinier_rg_errornull
pddf_dmax57.0
pddf_dmax_errornull
porod_volume89.2
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first2
guinier_point_last13
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDA77_datloglog_img.png
symmetrynull
last_modified2023-06-21T07:56:39.492710+02:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDA77
statussuccess
started_at2026-08-11T15:23:19.960687+00:00
finished_at2026-08-11T15:23:29.480736+00:00
source_last_modified2023-06-21T07:56:39.492710+02:00
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View the complete summary.json source
{
  "code": "SASDA77",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/nm",
  "project": {
    "title": "Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein.",
    "publication": {
      "title": "Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein.",
      "author_list": "Gruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J",
      "journal": "Nat Commun",
      "doi": "10.1038/ncomms8271",
      "pmid": "26027519",
      "published_date": "2015 Jun 1"
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View the complete manifest.json source
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