2. Measurements Reported by SASBDB Reported Results
Metric
Method
Value
Uncertainty
Unit
mw
Experimental
43.0
—
kDa
rg
P(r)
4.0
—
Å
These values are reported by SASBDB; SAXSdb did not recalculate them from the experimental curve.
▼
3. Source Fits and Models Source Fits & Models
This entry has no source fit record.
▶
4. Source File Index Source Files
Category
Path
Download status
Size
curve
sasbdb/entries/v8/sasddv8/source/SASDDV8.dat
downloaded
7303
full_entry_zip
sasbdb/entries/v8/sasddv8/source/SASDDV8.zip
downloaded
1896
pddf
sasbdb/entries/v8/sasddv8/source/SASDDV8.out
not_listed
—
sascif
sasbdb/entries/v8/sasddv8/source/SASDDV8.sascif
downloaded
13992
summary
sasbdb/entries/v8/sasddv8/source/summary.json
downloaded
7078
▶
5. Experiment Description and Publication Experiment & Publication
Original Experiment Description
This data set displays SAXS data measured from egg albumen of a hard-boiled chicken egg. The most abundant protein in the egg white is ovalbumin, but there are other proteins present as well. After hard boiling, the egg proteins completely unfolded, resulting in a white gel. Because the proteins strongly interact to form extended materials, the parameters Rg and monomer molecular weight do not apply to this sample. 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 sample measurement (1 x 1800 s exposure) was performed at 10°C. Measurements used a rotating-anode system with Cu Kα radiation (λ = 0.1542 nm) from a Bruker-Nonius FR591 generator operated at 3.4 kW. Collimation was performed using circular pinholes and Osmic Max-Flux confocal optics. The scattered X-rays (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle) were collected using a Bruker Hi-Star area detector. Data were collected at sample−detector distances of 54 and 150 cm, and the data merged to create a single profile over the range q ∈ [0.08, 3.5] nm−1. To minimize background, an integral vacuum with a pressure of < 0.3 mbar was maintained along the entire flight path.
Related Publication
Title
The Proof Is in the <i>Pidan</i>: Generalizing Proteins as Patchy Particles.
Authors
Cai J, Sweeney AM
DOI / PMID
10.1021/acscentsci.8b00187 / 30062112
▼
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.
This data set displays SAXS data measured from egg albumen of a hard-boiled chicken egg. The most abundant protein in the egg white is ovalbumin, but there are other proteins present as well. After hard boiling, the egg proteins completely unfolded, resulting in a white gel. Because the proteins strongly interact to form extended materials, the parameters Rg and monomer molecular weight do not apply to this sample. 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 sample measurement (1 x 1800 s exposure) was performed at 10°C. Measurements used a rotating-anode system with Cu Kα radiation (λ = 0.1542 nm) from a Bruker-Nonius FR591 generator operated at 3.4 kW. Collimation was performed using circular pinholes and Osmic Max-Flux confocal optics. The scattered X-rays (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle) were collected using a Bruker Hi-Star area detector. Data were collected at sample−detector distances of 54 and 150 cm, and the data merged to create a single profile over the range q ∈ [0.08, 3.5] nm−1. To minimize background, an integral vacuum with a pressure of < 0.3 mbar was maintained along the entire flight path.
{
"code": "SASDDV8",
"status": "Published",
"type_of_curve": "Merged",
"angular_unit": "1/A",
"project": {
"title": "The Proof Is in the <i>Pidan</i>: Generalizing Proteins as Patchy Particles.",
"publication": {
"title": "The Proof Is in the <i>Pidan</i>: Generalizing Proteins as Patchy Particles.",
"author_list": "Cai J, Sweeney AM",
"journal": "ACS Cent Sci",
"doi": "10.1021/acscentsci.8b00187",
"pmid": "30062112",
"published_date": "2018 Jul 25"
},
"status": "released",
"submitted_date": "2018-06-23",
"released_date": "2018-07-20"
},
"pddf_data": null,
"intensities_data": "https://www.sasbdb.org/media/intensities_files/SASDDV8.dat",
"intensities_log_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDDV8_dat_img.png",
"intensities_kratky_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDDV8_kratky_img.png",
"pddf_plot": null,
"intensities_guinier_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDDV8_guinier_img.png",
"sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDDV8.sascif",
"experiment": {
"instrument": {
"detector": {
"type": "multiwire",
"name": "Bruker HI-STAR",
"resolution": 0.0
},
"name": "University of Pennslyvania",
"city": "Philadelphia, PA",
"country": "USA",
"beamline_name": "Bruker Nonius FR591",
"beam_geometry": null,
"type_of_source": "X-ray in house",
"point_source": null,
"line_collimation": null,
"sample_path_length": null,
"line_collimation_slitlength": null,
"line_collimation_integrationwidth": null,
"xray_energy": null,
"beam_profile_ah": null,
"beam_profile_al": null
},
"sample": {
"molecule": [
{
"long_name": "Ovalbumin",
"short_name": "Ova",
"sequence": "GSIGAASMEFCFDVFKELKVHHANENIFYCPIAIMSALAMVYLGAKDSTRTQINKVVRFDKLPGFGDSIEAQCGTSVNV\r\nHSSLRDILNQITKPNDVYSFSLASRLYAEERYPILPEYLQCVKELYRGGLEPINFQTAADQARELINSWVESQTNGIIRN\r\nVLQPSSVDSQTAMVLVNAIVFKGLWEKAFKDEDTQAMPFRVTEQESKPVQMMYQIGLFRVASMASEKMKILELPFASGTM\r\nSMLVLLPDEVSGLEQLESIINFEKLTEWTSSNVMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDVFSSSANLSGISSAE\r\nSLKISQAVHAAHAEINEAGREVVGSAEAGVDAASVSEEFRADHPFLFCIKHIATNAVLFFGRCVSP",
"organism": "Gallus gallus",
"uniprot_code": "P01012",
"uniprot_range_first": null,
"uniprot_range_last": null,
"oligomerization": "monomer",
"molecular_type": "protein",
"uniprot_sequence": "MGSIGAASMEFCFDVFKELKVHHANENIFYCPIAIMSALAMVYLGAKDSTRTQINKVVRF\nDKLPGFGDSIEAQCGTSVNVHSSLRDILNQITKPNDVYSFSLASRLYAEERYPILPEYLQ\nCVKELYRGGLEPINFQTAADQARELINSWVESQTNGIIRNVLQPSSVDSQTAMVLVNAIV\nFKGLWEKAFKDEDTQAMPFRVTEQESKPVQMMYQIGLFRVASMASEKMKILELPFASGTM\nSMLVLLPDEVSGLEQLESIINFEKLTEWTSSNVMEERKIKVYLPRMKMEEKYNLTSVLMA\nMGITDVFSSSANLSGISSAESLKISQAVHAAHAEINEAGREVVGSAEAGVDAASVSEEFR\nADHPFLFCIKHIATNAVLFFGRCVSP",
"mw": 42.75,
"total_mw": 42.75,
"number_molecules": 1,
"complex_state": false,
"deuteration": null,
"molecule_source": "biological",
"molecule_description": null
}
],
"buffer": {
"name": "Water",
"concentration_unit": null,
"comment": null,
"additive": null,
"concentration": null,
"pka": null,
"ph": 7.0,
"deuteration": null
},
"purity_method": null,
"name": "Boiled chicken egg albumen",
"ext_coefficient": null,
"contrast": null,
"specific_vol": null,
"dry_vol": null,
"absorbption": null,
"deuteration": null,
"mixture": null
},
"contributor": [
{
"affiliation": [
{
"short_name": "Penn",
"address": "Philadelphia, PA, United States",
"full_name": "University of Pennsylvania",
"webpage": "http://www.upenn.edu/"
}
],
"contributor_name": "Jing",
"contributor_surname": "Cai",
"orcid": null
}
],
"concentration_method": null,
"concentration_unit": null,
"date": "2013-06-27",
"storage_temperature": 4.0,
"cell_temperature": 10.0,
"exposure_time": 1800.0,
"number_of_frames": 1,
"wavelength": 0.1542,
"sample_detector_distance": 1.5,
"concentration_min": null,
"concentration_max": 170.0,
"sample_volume": null,
"flow_rate": null,
"s_min": 0.08,
"s_max": 3.28,
"total_exposure_time": null,
"seccolumn": null
},
"fits": [],
"estimated_volume_method": null,
"pddf_software": null,
"pddf_software_version": null,
"i0_calibration_standard": null,
"description": null,
"experiment_description": "This data set displays SAXS data measured from egg albumen of a hard-boiled chicken egg. The most abundant protein in the egg white is ovalbumin, but there are other proteins present as well. After hard boiling, the egg proteins completely unfolded, resulting in a white gel. Because the proteins strongly interact to form extended materials, the parameters Rg and monomer molecular weight do not apply to this sample. 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 sample measurement (1 x 1800 s exposure) was performed at 10°C. Measurements used a rotating-anode system with Cu Kα radiation (λ = 0.1542 nm) from a Bruker-Nonius FR591 generator operated at 3.4 kW. Collimation was performed using circular pinholes and Osmic Max-Flux confocal optics. The scattered X-rays (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle) were collected using a Bruker Hi-Star area detector. Data were collected at sample−detector distances of 54 and 150 cm, and the data merged to create a single profile over the range q ∈ [0.08, 3.5] nm−1. To minimize background, an integral vacuum with a pressure of < 0.3 mbar was maintained along the entire flight path.",
"tags": [
"softmatter"
],
"intensity_unit": "arbitrary",
"experimental_mw": 43.0,
"experimental_mw_error": null,
"guinier_i0_mw": null,
"guinier_i0_mw_error": null,
"porod_mw": null,
"porod_mw_error": null,
"pddf_i0": null,
"pddf_i0_error": null,
"guinier_i0": null,
"guinier_i0_error": null,
"pddf_rg": 4.0,
"pddf_rg_error": null,
"guinier_rg": null,
"guinier_rg_error": null,
"pddf_dmax": null,
"pddf_dmax_error": null,
"porod_volume": null,
"porod_volume_error": null,
"estimated_volume": null,
"estimated_volume_error": null,
"guinier_point_first": null,
"guinier_point_last": null,
"pddf_point_first": null,
"pddf_point_last": null,
"i0_calibration_standard_data": null,
"intensities_log_log_plot": "SASDDV8_datloglog_img.png",
"symmetry": null,
"last_modified": "2022-01-27T08:13:53.938538+01:00",
"bragg_peak": []
}
