SASDV62

Human Haemoglobin (Sigma-Aldrich) in 100mM Sodium Phosphate buffer, pH=7.0, SEC-SAXS

Data type: SASBDB experimental data Status: Published Curve type: SEC-SAS 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) in 100mM Sodium Phosphate buffer, pH=7.0, SEC-SAXS

Concentration— – 18.0 Buffer / pH100 mM Sodium Phosphate / 7.0
Experimental temperature20.0 Facility / beamlineInstitute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure / Anton Paar SAXSpoint 2.0
Wavelength1.34 nmExposure15.0 s × 106

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
1680[3]0.08863436–3.997122 1/nmHas uncertainty columnMissing 039sasbdb/entries/62/sasdv62/source/SASDV62.dat
▼

2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)6.8—nm
i0Guinier0.196231—arbitrary
i0P(r)0.19530.0004arbitrary
mwExperimental64848.0—kDa
mwPorod56.0—kDa
porod_volumePorod105.0—nm³
rgGuinier2.420.01nm
rgP(r)2.380.005nm

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 name100 mM Sodium PhosphateBuffer concentration—
pH7.0Additives—
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2022-05-24Storage / measurement temperature23.0 / 20.0
Exposure time15.0Frames106
Wavelength1.34Sample-to-detector distance0.7926
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 range0.089 – 3.997Sample volume / flow rate500.0 / 0.05

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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pddf: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:216 field values
Field pathRaw value
codeSASDV62
statusPublished
type_of_curveSEC-SAS
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
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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.name100 mM Sodium Phosphate
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameHuman Haemoglobin (Sigma-Aldrich) in 100mM Sodium Phosphate buffer, pH=7.0, SEC-SAXS
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.date2022-05-24
experiment.storage_temperature23.0
experiment.cell_temperature20.0
experiment.exposure_time15.0
experiment.number_of_frames106
experiment.wavelength1.34
experiment.sample_detector_distance0.7926
experiment.concentration_minnull
experiment.concentration_max18.0
experiment.sample_volume500.0
experiment.flow_rate0.05
experiment.s_min0.089
experiment.s_max3.997
experiment.total_exposure_timenull
experiment.seccolumn1
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fits[0].softwareDAMMIN
fits[0].chi_square_value1.043
fits[0].p_value0.5562
fits[0].fit_residual_plotSASDV62_fit1_fitresiduals_img.png
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fits[0].description
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fits[1].chi_square_value1.098
fits[1].p_value0.8103
fits[1].fit_residual_plotSASDV62_fit2_fitresiduals_img.png
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fits[1].description
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pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionExperimental molecular weight: Size&Shape value from PRIMUS was used.
experiment_descriptionnull
tags[]
intensity_unitarbitrary
experimental_mw64848.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw56.0
porod_mw_errornull
pddf_i00.1953
pddf_i0_error0.0004
guinier_i00.196231
guinier_i0_errornull
pddf_rg2.38
pddf_rg_error0.005
guinier_rg2.42
guinier_rg_error0.01
pddf_dmax6.8
pddf_dmax_errornull
porod_volume105.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first5
guinier_point_last78
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDV62_datloglog_img.png
symmetrynull
last_modified2024-10-24T13:24:24.520562+02:00
bragg_peak[]
manifest.json:34 field values
Field pathRaw value
codeSASDV62
statussuccess
started_at2026-08-11T13:31:42.589595+00:00
finished_at2026-08-11T13:31:52.147967+00:00
source_last_modified2024-10-24T13:24:24.520562+02:00
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View the complete summary.json source
{
  "code": "SASDV62",
  "status": "Published",
  "type_of_curve": "SEC-SAS",
  "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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  "experiment": {
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View the complete manifest.json source
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