This data set displays SAXS data measured from the egg white from a Chinese century egg (pidan) prepared from quail eggs. The most abundant protein in the egg white is ovalbumin, but there are other proteins present. The pidan was prepared by soaking eggs in 0.9 M NaOH and 0.5 M NaCl for three weeks. The egg white formed a transparent gel during this process. The egg proteins experienced a partial unfolding and formed intermolecular cross-links. Because the proteins link to form extended materials, the parameter Rg and monomer molecular weight does not apply here. 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.
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标题
The Proof Is in the <i>Pidan</i>: Generalizing Proteins as Patchy Particles.
This data set displays SAXS data measured from the egg white from a Chinese century egg (pidan) prepared from quail eggs. The most abundant protein in the egg white is ovalbumin, but there are other proteins present. The pidan was prepared by soaking eggs in 0.9 M NaOH and 0.5 M NaCl for three weeks. The egg white formed a transparent gel during this process. The egg proteins experienced a partial unfolding and formed intermolecular cross-links. Because the proteins link to form extended materials, the parameter Rg and monomer molecular weight does not apply here. 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": "SASDDW8",
"status": "Published",
"type_of_curve": "Single concentration",
"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/SASDDW8.dat",
"intensities_log_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDDW8_dat_img.png",
"intensities_kratky_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDDW8_kratky_img.png",
"pddf_plot": null,
"intensities_guinier_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDDW8_guinier_img.png",
"sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDDW8.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 (common quail)",
"short_name": "Ova",
"sequence": "GSIGAASMEFCFDVFKELKVHHANDNMLYSPFAILSTLAMVFLGAKDSTRTQINKVVHFDKLPGFGDSI\r\nEAQCGTSANVHSSLRDILNQITKQNDAYSFSLASRLYAQETYTVVPEYLQCVKELYRGGLESVNFQTAAD\r\nQARGLINAWVESQTNGIIRNILQPSSVDSQTAMVLVNAIAFKGLWEKAFKAEDTQTIPFRVTEQESKPVQ\r\nMMHQIGSFKVASMASEKMKILELPFASGTMSMLVLLPDDVSGLEQLESTISFEKLTEWTSSSIMEERKVK\r\nVYLPRMKMEEKYNLTSLLMAMGITDLFSSSANLSGISSVGSLKIPQAVHAAYAEINEAGRDVVGSAEAGV\r\nDATEEFRADHPFLFCVKHIETNAILLFGRCVSP",
"organism": "Coturnix coturnix",
"uniprot_code": "Q6V115",
"uniprot_range_first": null,
"uniprot_range_last": null,
"oligomerization": "monomer",
"molecular_type": "protein",
"uniprot_sequence": "MGSIGAASMEFCFDVFKELKVHHANDNMLYSPFAILSTLAMVFLGAKDSTRTQINKVVHF\nDKLPGFGDSIEAQCGTSANVHSSLRDILNQITKQNDAYSFSLASRLYAQETYTVVPEYLQ\nCVKELYRGGLESVNFQTAADQARGLINAWVESQTNGIIRNILQPSSVDSQTAMVLVNAIA\nFKGLWEKAFKAEDTQTIPFRVTEQESKPVQMMHQIGSFKVASMASEKMKILELPFASGTM\nSMLVLLPDDVSGLEQLESTISFEKLTEWTSSSIMEERKVKVYLPRMKMEEKYNLTSLLMA\nMGITDLFSSSANLSGISSVGSLKIPQAVHAAYAEINEAGRDVVGSAEAGVDATEEFRADH\nPFLFCVKHIETNAILLFGRCVSP",
"mw": 42.078,
"total_mw": 42.078,
"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": "Chinese century egg albumen (pidan) made from quail egg",
"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 the egg white from a Chinese century egg (pidan) prepared from quail eggs. The most abundant protein in the egg white is ovalbumin, but there are other proteins present. The pidan was prepared by soaking eggs in 0.9 M NaOH and 0.5 M NaCl for three weeks. The egg white formed a transparent gel during this process. The egg proteins experienced a partial unfolding and formed intermolecular cross-links. Because the proteins link to form extended materials, the parameter Rg and monomer molecular weight does not apply here. 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": 42.0,
"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": 1.0,
"guinier_i0_error": null,
"pddf_rg": null,
"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": "SASDDW8_datloglog_img.png",
"symmetry": null,
"last_modified": "2022-01-27T08:14:23.545135+01:00",
"bragg_peak": []
}
