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Yorodumi- SASDF99: Bovine serum albumin monomer - SEC-SAXS/WAXS coupled to multiangl... -
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Basic information
| Entry | Database: SASBDB / ID: SASDF99 |
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Sample | 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 | Function and homology informationcellular 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 |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
-Data source
| SASBDB page | SASDF99 |
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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 Search similar-shape structures of this assembly by Omokage search (details) |
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| Model #3560 | ![]() Type: atomic / Radius of dummy atoms: 1.90 A / Chi-square value: 2.417 Search similar-shape structures of this assembly by Omokage search (details) |
| Model #3559 | ![]() Type: atomic / Symmetry: P1 / Chi-square value: 1.548 / P-value: 0.033334 Search similar-shape structures of this assembly by Omokage search (details) |
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Sample
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 / Type of source: X-ray synchrotron / Wavelength: 0.124 Å / Dist. spec. to detc.: 1 mm | ||||||||||||||||||||||||||||||
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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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