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- SASDF99: Bovine serum albumin monomer - SEC-SAXS/WAXS coupled to multiangl... -
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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDF99 |
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![]() | Bovine serum albumin monomer - SEC-SAXS/WAXS coupled to multiangle laser and quasi-elastic light scattering (MALLS and QELS)
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Function / homology | ![]() cellular response to calcium ion starvation / enterobactin binding / negative regulation of mitochondrial depolarization / toxic substance binding / cellular response to starvation / fatty acid binding / pyridoxal phosphate binding / protein-containing complex / DNA binding / extracellular space ...cellular response to calcium ion starvation / enterobactin binding / negative regulation of mitochondrial depolarization / toxic substance binding / cellular response to starvation / fatty acid binding / pyridoxal phosphate binding / protein-containing complex / DNA binding / extracellular space / extracellular region / metal ion binding / cytoplasm Similarity search - Function |
Biological species | ![]() ![]() |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
-Data source
SASBDB page | ![]() |
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-Related structure data
Similar structure data |
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External links
Related items in Molecule of the Month |
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-Models
Model #3558 | ![]() Type: dummy / Software: (2.3i) / Radius of dummy atoms: 1.90 A / Symmetry: P1 / Chi-square value: 1.45 / P-value: 0.298705 ![]() |
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Model #3560 | ![]() Type: atomic / Radius of dummy atoms: 1.90 A / Chi-square value: 2.417 ![]() |
Model #3559 | ![]() Type: atomic / Symmetry: P1 / Chi-square value: 1.548 / P-value: 0.033334 ![]() |
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Sample
![]() | Name: Bovine serum albumin monomer - SEC-SAXS/WAXS coupled to multiangle laser and quasi-elastic light scattering (MALLS and QELS) Specimen concentration: 15 mg/ml |
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Buffer | Name: 50 mM HEPES, 3% v/v glycerol, / pH: 7.5 |
Entity #1306 | Name: 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 |
-Experimental information
Beam | Instrument name: PETRA III EMBL P12 / City: Hamburg / 国: Germany ![]() | ||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 2M | ||||||||||||||||||||||||||||||
Scan | Measurement date: Apr 23, 2017 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 63 / Unit: 1/nm /
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Distance distribution function P(R) |
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Result | Comments: Protein powder (Sigma) consisting of BSA monomers, dimers, trimers and higher MW species was dissolved in the SEC-running buffer and then 0.22 micon spin filtered prior to injection onto ...Comments: Protein powder (Sigma) consisting of BSA monomers, dimers, trimers and higher MW species was dissolved in the SEC-running buffer and then 0.22 micon spin filtered prior to injection onto the SEC column. The sample injection 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). The Rg-correlation through the SEC-SAXS/WAXS peak, the individual unsubtracted SEC-SAXS/WAXS 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 from the separated monomer peak using MALLS in combination with refractive-index (RI) measurements from the same sample eluting from the column using a split-flow SEC-SAXS/WAXS-light scattering configuration (Graewert et al., (2015) Sci. Reports. 5, 10734: doi: 10.1038/srep10734). The average hydrodynamic radius of the separated monomer was evaluated at 3.4 nm. Two atomistic representations of the protein are displayed: 1) The X-ray crystallography model fit to the SAXS data (PDB:4F5S), middle, and; 2) The same model after normal mode analysis/refinement using SREFLEX (bottom; Panjkovich et al., (2016) Phys. Chem. Chem. Phys. 18(8):5707-5719. doi: 10.1039/c5cp04540a). The complete SREFLEX result summary is included in the full-entry zip archive.
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