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- SASDFQ8: Bovine serum albumin, purified monomer - SEC-SAXS coupled to mult... -

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ID or keywords:

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Basic information

Entry
Database: SASBDB / ID: SASDFQ8
SampleBovine serum albumin, purified monomer - SEC-SAXS coupled to multiangle laser and quasi-elastic light scattering (MALLS and QELS)
  • Bovine serum albumin (protein), BSA, Bos taurus
Function / homology
Function and homology information


cellular response to calcium ion starvation / enterobactin binding / negative regulation of mitochondrial depolarization / toxic substance binding / fatty acid binding / cellular response to starvation / pyridoxal phosphate binding / protein-containing complex / extracellular space / DNA binding ...cellular response to calcium ion starvation / enterobactin binding / negative regulation of mitochondrial depolarization / toxic substance binding / fatty acid binding / cellular response to starvation / pyridoxal phosphate binding / protein-containing complex / extracellular space / DNA binding / extracellular region / metal ion binding / cytoplasm
Similarity search - Function
Serum albumin/Alpha-fetoprotein/Afamin / ALB/AFP/VDB / Serum albumin, N-terminal / Serum albumin, conserved site / Serum albumin-like / Serum albumin family / Albumin domain signature. / Albumin domain profile. / serum albumin
Similarity search - Domain/homology
Biological speciesBos taurus (domestic cattle)
Contact author
  • Melissa Graewert
  • Cy M Jeffries

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Models

Model #3519
Type: dummy / Radius of dummy atoms: 1.90 A / Symmetry: P1 / Chi-square value: 1.15 / P-value: 0.041814
Search similar-shape structures of this assembly by Omokage search (details)
Model #3523
Type: atomic / Radius of dummy atoms: 1.90 A / Chi-square value: 1.332
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Bovine serum albumin, purified monomer - SEC-SAXS coupled to multiangle laser and quasi-elastic light scattering (MALLS and QELS)
Specimen concentration: 8.8 mg/ml
BufferName: 50 mM HEPES, 150 mM NaCl, 2% v/v glycerol, / pH: 7 / Comment: Running buffer for SEC-SAXS
Entity #1306Name: BSA / Type: protein / Description: Bovine serum albumin / Formula weight: 66.432 / Num. of mol.: 1 / Source: Bos taurus / References: UniProt: P02769
Sequence: DTHKSEIAHR FKDLGEEHFK GLVLIAFSQY LQQCPFDEHV KLVNELTEFA KTCVADESHA GCEKSLHTLF GDELCKVASL RETYGDMADC CEKQEPERNE CFLSHKDDSP DLPKLKPDPN TLCDEFKADE KKFWGKYLYE IARRHPYFYA PELLYYANKY NGVFQECCQA ...Sequence:
DTHKSEIAHR FKDLGEEHFK GLVLIAFSQY LQQCPFDEHV KLVNELTEFA KTCVADESHA GCEKSLHTLF GDELCKVASL RETYGDMADC CEKQEPERNE CFLSHKDDSP DLPKLKPDPN TLCDEFKADE KKFWGKYLYE IARRHPYFYA PELLYYANKY NGVFQECCQA EDKGACLLPK IETMREKVLA SSARQRLRCA SIQKFGERAL KAWSVARLSQ KFPKAEFVEV TKLVTDLTKV HKECCHGDLL ECADDRADLA KYICDNQDTI SSKLKECCDK PLLEKSHCIA EVEKDAIPEN LPPLTADFAE DKDVCKNYQE AKDAFLGSFL YEYSRRHPEY AVSVLLRLAK EYEATLEECC AKDDPHACYS TVFDKLKHLV DEPQNLIKQN CDQFEKLGEY GFQNALIVRY TRKVPQVSTP TLVEVSRSLG KVGTRCCTKP ESERMPCTED YLSLILNRLC VLHEKTPVSE KVTKCCTESL VNRRPCFSAL TPDETYVPKA FDEKLFTFHA DICTLPDTEK QIKKQTALVE LLKHKPKATE EQLKTVMENF VAFVDKCCAA DDKEACFAVE GPKLVVSTQT ALA

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Experimental information

BeamInstrument name: PETRA III EMBL P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotron / Wavelength: 0.123982 Å / Dist. spec. to detc.: 3 mm
DetectorName: Pilatus 6M
Scan
Title: Bovine serum albumin, purified monomer - SEC-SAXS coupled to multiangle laser and quasi-elastic light scattering (MALLS and QELS)
Measurement date: Apr 5, 2019 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 81 / Unit: 1/nm /
MinMax
Q0.0979 7.213
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 1413 /
MinMax
Q0.097859 4.00096
P(R) point1 1413
R0 8
Result
Type of curve: sec
Comments: BSA monomer underwent pre-purification prior to SEC-SAXS using the following method. All procedures were performed at 4 oC. Protein powder (Sigma) consisting of BSA monomers, dimers, ...Comments: BSA monomer underwent pre-purification prior to SEC-SAXS using the following method. All procedures were performed at 4 oC. Protein powder (Sigma) consisting of BSA monomers, dimers, trimers and higher MW species was made to approximately 25 mg/ml in 25 mM HEPES, 50 mM NaCl, 5 mM urea, 1% v/v glycerol, pH 7. Approximately 200 μl of sample were loaded onto a Superdex 200 Increase 10/300 column (GE Healthcare) equilibrated in the same buffer (flow rate = 0.4 ml/min). Fractionated aliquots corresponding to the highest absorbing peak (estimated using UV A280 and UV A245 nm) were pooled and concentrated (30 kDa centrifuge spin filter) to a final concentration of 8.8 mg/ml (the concentration was determined from triplicate UV A280 measurements using an E0.1% of 0.646 (= 1 g/l) calculated from the amino acid sequence (ProtParam)). Approximately 75 μl aliquots were snap-frozen in liquid nitrogen then stored at -80oC prior to the SEC-SAXS analysis that was performed at room temperature in 50 mM HEPES, 150 mM NaCl, 2% v/v glycerol, pH 7. The Rg-correlation through the SEC-SAXS peak, the individual unsubtracted SEC-SAXS frames as well as the results from coupled MALLS and QELS analysis are included in the full entry zip archive. The quoted experimental molecular weight was determined using MALLS in combination with refractive-index (RI) measurements that were recorded from the same sample eluting from the column using a split-flow SEC-SAXS-light scattering configuration (Graewert et al., (2015) Sci. Reports. 5, 10734: doi: 10.1038/srep10734). The average hydrodynamic radius of the protein is 3.5 nm.
ExperimentalPorod
MW63 kDa62 kDa
Volume-98.4 nm3

P(R)GuinierGuinier error
Forward scattering, I015430 15415.7 5.9
Radius of gyration, Rg2.752 nm2.76 nm-

MinMax
D-8
Guinier point1 135

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