SASDVD2

Human Haemoglobin (Sigma-Aldrich) with 5% (w/v) PEG4000 in 100mM Sodium Phosphate buffer, pH=7.0, c=5mg/ml

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2024-10-24T13:24:24.520562+02:00

Experimental molecular weight: Size&Shape value from PRIMUS was used.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Human Haemoglobin (Sigma-Aldrich) with 5% (w/v) PEG4000 in 100mM Sodium Phosphate buffer, pH=7.0, c=5mg/ml

Concentration— – 5.0 Buffer / pH100mM Sodium Phosphate buffer with 5% (w/v) PEG4000 / 7.0
Experimental temperature20.0 Facility / beamlineInstitute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure / Anton Paar SAXSpoint 2.0
Wavelength1.34 nmExposure30.0 s × 30

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Hemoglobin subunit alpha
View sequence
VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR
proteinHomo sapiensP699052–142monomerMolecule count 115.126 kDa
Hemoglobin subunit beta
View sequence
VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
proteinHomo sapiensP688712–147monomerMolecule count 115.867 kDa
Protoporphyrin IX containing fe
View sequence
C34H32FEN4O4
other———–—monomerMolecule count 10.616 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
1681[3]0.08287812–3.997122 1/nmHas uncertainty columnMissing 0206sasbdb/entries/d2/sasdvd2/source/SASDVD2.dat
▼

2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)6.12—nm
i0Guinier0.0971725—1/cm
i0P(r)0.095950.00041/cm
mwExperimental59.0—kDa
mwPorod60.7—kDa
porod_volumePorod90.5—nm³
rgGuinier2.3880.026nm
rgP(r)2.3180.008nm

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.

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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 name100mM Sodium Phosphate buffer with 5% (w/v) PEG4000Buffer concentration—
pH7.0Additives—
Buffer description5% (w/v) PEG4000 is the final concentration.
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2022-10-06Storage / measurement temperature23.0 / 20.0
Exposure time30.0Frames30
Wavelength1.34Sample-to-detector distance0.8256
SourceX-ray in houseDetectorEiger R 1M
Facility / beamlineInstitute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure / Anton Paar SAXSpoint 2.0 · Vestec, Czech Republic
q range0.083 – 3.997Sample volume / flow rate500.0 / 0.7

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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summarysasbdb/entries/d2/sasdvd2/source/summary.jsondownloaded7585e3bc871441aa8881db684ec1e17275b88666ad5a8c7e5e4d4b5095fa90ddd6c2DownloadView source fileSource site
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full_entry_zip:source record and ZIP contents (2 items)
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pddf:source record
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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:168 field values
Field pathRaw value
codeSASDVD2
statusPublished
type_of_curveSingle concentration
angular_unit1/nm
project.titleHemoglobin–PEG Interactions Probed by Small-Angle X-ray Scattering: Insights for Crystallization and Diagnostics Applications
project.publication.titleHemoglobin–PEG Interactions Probed by Small-Angle X-ray Scattering: Insights for Crystallization and Diagnostics Applications
project.publication.author_listBaranova I, Angelova A, Stransky J, Andreasson J, Angelov B
project.publication.journalThe Journal of Physical Chemistry B
project.publication.doi10.1021/acs.jpcb.4c03003
project.publication.pmidnull
project.publication.published_date2024 Sep 09
project.statusreleased
project.submitted_date2024-05-28
project.released_date2024-09-10
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDVD2.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDVD2.dat
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intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDVD2_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDVD2_pofr_img.png
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sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDVD2.sascif
experiment.instrument.detector.typenull
experiment.instrument.detector.nameEiger R 1M
experiment.instrument.detector.resolution0.75
experiment.instrument.nameInstitute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure
experiment.instrument.cityVestec
experiment.instrument.countryCzech Republic
experiment.instrument.beamline_nameAnton Paar SAXSpoint 2.0
experiment.instrument.beam_geometrynull
experiment.instrument.type_of_sourceX-ray in house
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_nameHemoglobin subunit alpha
experiment.sample.molecule[0].short_namehuman HbA
experiment.sample.molecule[0].sequenceVLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHG KKVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTP AVHASLDKFLASVSTVLTSKYR
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeP69905
experiment.sample.molecule[0].uniprot_range_first2
experiment.sample.molecule[0].uniprot_range_last142
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMVLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHG KKVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTP AVHASLDKFLASVSTVLTSKYR
experiment.sample.molecule[0].mw15.126
experiment.sample.molecule[0].total_mw15.126
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_description
experiment.sample.molecule[1].long_nameHemoglobin subunit beta
experiment.sample.molecule[1].short_namehuman HbB
experiment.sample.molecule[1].sequenceVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPK VKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFG KEFTPPVQAAYQKVVAGVANALAHKYH
experiment.sample.molecule[1].organismHomo sapiens
experiment.sample.molecule[1].uniprot_codeP68871
experiment.sample.molecule[1].uniprot_range_first2
experiment.sample.molecule[1].uniprot_range_last147
experiment.sample.molecule[1].oligomerizationmonomer
experiment.sample.molecule[1].molecular_typeprotein
experiment.sample.molecule[1].uniprot_sequenceMVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPK VKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFG KEFTPPVQAAYQKVVAGVANALAHKYH
experiment.sample.molecule[1].mw15.867
experiment.sample.molecule[1].total_mw15.867
experiment.sample.molecule[1].number_molecules1
experiment.sample.molecule[1].complex_stateFalse
experiment.sample.molecule[1].deuterationnull
experiment.sample.molecule[1].molecule_sourcebiological
experiment.sample.molecule[1].molecule_description
experiment.sample.molecule[2].long_nameProtoporphyrin IX containing fe
experiment.sample.molecule[2].short_nameHeme B, Haem B
experiment.sample.molecule[2].sequenceC34H32FeN4O4
experiment.sample.molecule[2].organismnull
experiment.sample.molecule[2].uniprot_codenull
experiment.sample.molecule[2].uniprot_range_firstnull
experiment.sample.molecule[2].uniprot_range_lastnull
experiment.sample.molecule[2].oligomerizationmonomer
experiment.sample.molecule[2].molecular_typeother
experiment.sample.molecule[2].uniprot_sequence
experiment.sample.molecule[2].mw0.616
experiment.sample.molecule[2].total_mw0.616
experiment.sample.molecule[2].number_molecules1
experiment.sample.molecule[2].complex_stateFalse
experiment.sample.molecule[2].deuterationnull
experiment.sample.molecule[2].molecule_sourcebiological
experiment.sample.molecule[2].molecule_descriptionCAS: 104244-10-2 ECSA: 600-546-5 IUPAC: 3-[18-(2-carboxyethyl)-8,13-bis(ethenyl)-3,7,12,17-tetramethylporphyrin-21,23-diid-2-yl]propanoic acid;iron(2+)
experiment.sample.buffer.name100mM Sodium Phosphate buffer with 5% (w/v) PEG4000
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.comment5% (w/v) PEG4000 is the final concentration.
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameHuman Haemoglobin (Sigma-Aldrich) with 5% (w/v) PEG4000 in 100mM Sodium Phosphate buffer, pH=7.0, c=5mg/ml
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_nameThe Extreme Light Infrastructure ERIC
experiment.contributor[0].affiliation[0].webpagenull
experiment.contributor[0].contributor_nameIuliia
experiment.contributor[0].contributor_surnameBaranova
experiment.contributor[0].orcidhttps://orcid.org/0009-0003-2262-2054
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2022-10-06
experiment.storage_temperature23.0
experiment.cell_temperature20.0
experiment.exposure_time30.0
experiment.number_of_frames30
experiment.wavelength1.34
experiment.sample_detector_distance0.8256
experiment.concentration_minnull
experiment.concentration_max5.0
experiment.sample_volume500.0
experiment.flow_rate0.7
experiment.s_min0.083
experiment.s_max3.997
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionExperimental molecular weight: Size&Shape value from PRIMUS was used.
experiment_descriptionnull
tags[]
intensity_unit1/cm
experimental_mw59.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw60.7
porod_mw_errornull
pddf_i00.09595
pddf_i0_error0.0004
guinier_i00.0971725
guinier_i0_errornull
pddf_rg2.318
pddf_rg_error0.008
guinier_rg2.388
guinier_rg_error0.026
pddf_dmax6.12
pddf_dmax_errornull
porod_volume90.5
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first11
guinier_point_last80
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDVD2_datloglog_img.png
symmetrynull
last_modified2024-10-24T13:24:24.520562+02:00
bragg_peak[]
manifest.json:34 field values
Field pathRaw value
codeSASDVD2
statussuccess
started_at2026-08-11T13:36:32.828413+00:00
finished_at2026-08-11T13:36:40.376388+00:00
source_last_modified2024-10-24T13:24:24.520562+02:00
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View the complete summary.json source
{
  "code": "SASDVD2",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/nm",
  "project": {
    "title": "Hemoglobin–PEG Interactions Probed by Small-Angle X-ray Scattering: Insights for Crystallization and Diagnostics Applications",
    "publication": {
      "title": "Hemoglobin–PEG Interactions Probed by Small-Angle X-ray Scattering: Insights for Crystallization and Diagnostics Applications",
      "author_list": "Baranova I, Angelova A, Stransky J, Andreasson J, Angelov B",
      "journal": "The Journal of Physical Chemistry B",
      "doi": "10.1021/acs.jpcb.4c03003",
      "pmid": null,
      "published_date": "2024 Sep 09"
    },
    "status": "released",
    "submitted_date": "2024-05-28",
    "released_date": "2024-09-10"
  },
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      },
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      "city": "Vestec",
      "country": "Czech Republic",
      "beamline_name": "Anton Paar SAXSpoint 2.0",
      "beam_geometry": null,
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    "sample": {
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          "uniprot_range_first": 2,
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          "complex_state": false,
          "deuteration": null,
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          "molecule_description": ""
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          "uniprot_range_last": 147,
          "oligomerization": "monomer",
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          "complex_state": false,
          "deuteration": null,
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          "molecule_description": ""
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        {
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View the complete manifest.json source
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