SASDCJ3: Bovine Serum Albumin (Serum albumin)

Basic information

• Entry: Database: SASBDB / ID: SASDCJ3

Sample

Bovine Serum Albumin

• Serum albumin (protein), Bos taurus

Function / homology

Function:

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

Domain/homology:

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

Component:

Albumin

• Biological species: Bos taurus (domestic cattle)
• Citation: Journal: Acta Crystallogr D Struct Biol / Year: 2017; Title: 2017 publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution: an update.; Authors: Jill Trewhella / Anthony P Duff / Dominique Durand / Frank Gabel / J Mitchell Guss / Wayne A Hendrickson / Greg L Hura / David A Jacques / Nigel M Kirby / Ann H Kwan / Javier Pérez / Lois Pollack / Timothy M Ryan / Andrej Sali / Dina Schneidman-Duhovny / Torsten Schwede / Dmitri I Svergun / Masaaki Sugiyama / John A Tainer / Patrice Vachette / John Westbrook / Andrew E Whitten / ; Abstract: In 2012, preliminary guidelines were published addressing sample quality, data acquisition and reduction, presentation of scattering data and validation, and modelling for biomolecular small-angle scattering (SAS) experiments. Biomolecular SAS has since continued to grow and authors have increasingly adopted the preliminary guidelines. In parallel, integrative/hybrid determination of biomolecular structures is a rapidly growing field that is expanding the scope of structural biology. For SAS to contribute maximally to this field, it is essential to ensure open access to the information required for evaluation of the quality of SAS samples and data, as well as the validity of SAS-based structural models. To this end, the preliminary guidelines for data presentation in a publication are reviewed and updated, and the deposition of data and associated models in a public archive is recommended. These guidelines and recommendations have been prepared in consultation with the members of the International Union of Crystallography (IUCr) Small-Angle Scattering and Journals Commissions, the Worldwide Protein Data Bank (wwPDB) Small-Angle Scattering Validation Task Force and additional experts in the field.

Contact author

• Jill Trewhella (School of Molecular Bioscience, University of Sydney., Sydney, New South Wales 2006, Australia)

Models

• Model #1249: ; Type: dummy / Software: (on-line) / Radius of dummy atoms: 2.20 A / Symmetry: P1 / Chi-square value: 0.853 / P-value: 0.156000; Search similar-shape structures of this assembly by Omokage search (details)
• Model #1251: ; Type: atomic / Software: (on-line) / Radius of dummy atoms: 1.90 A / Symmetry: P1; Comment: Multi-FoXS 1-state model based on PDB:4F5S chain A with residues 187-183 & 381-384 flexible; Chi-square value: 1.05151837959 / P-value: 0.023000; Search similar-shape structures of this assembly by Omokage search (details)
• Model #1254: ; Type: atomic / Software: (on-line) / Radius of dummy atoms: 1.90 A / Symmetry: P1; Comment: Multi-FoXS e1-0 3-state model based on PDB:4F5S chain A with residues 187-183 & 381-384 flexible; Chi-square value: 0.836161911667 / P-value: 0.170900; Search similar-shape structures of this assembly by Omokage search (details)
• Model #1255: ; Type: atomic / Software: (on-line) / Radius of dummy atoms: 1.90 A / Symmetry: P1; Comment: Multi-FoXS e1-1 3-state model based on PDB:4F5S chain A with residues 187-183 & 381-384 flexible; Chi-square value: 0.836161911667 / P-value: 0.170900; Search similar-shape structures of this assembly by Omokage search (details)
• Model #1256: ; Type: atomic / Software: (on-line) / Radius of dummy atoms: 1.90 A / Symmetry: P1; Comment: Multi-FoXS e1-2 3-state model based on PDB:4F5S chain A with residues 187-183 & 381-384 flexible; Chi-square value: 0.836161911667 / P-value: 0.170900; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Bovine Serum Albumin / Specimen concentration: 0.56 mg/ml
• Buffer: Name: 25 mM MOPS, 250 mM NaCl, 50 mM KCl, 2 mM TCEP, 0.1% NaN3; pH: 7.5

Entity #671

Type: protein / Description: 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 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: Australian Synchrotron SAXS/WAXS / City: Melbourne / 国: Australia / Shape: Point / Type of source: X-ray synchrotron / Wavelength: 0.10332 Å / Dist. spec. to detc.: 2.683 mm
• Detector: Name: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm

Scan

Title: Bovine Serum Albumin / Measurement date: Mar 9, 2017 / Cell temperature: 22 °C / Exposure time: 1 sec. / Number of frames: 24 / Unit: 1/A /

	Min	Max
Q	0.0066	0.3104

Distance distribution function P(R)

Sofotware P(R): GNOM 5.0 / Number of points: 354 /

	Min	Max
Q	0.00662753	0.281638
P(R) point	1	354
R	0	87.03

Result

Type of curve: single_conc

	Experimental	Standard	Porod
MW	66.43 kDa	65.12 kDa	67.333 kDa
Volume	-	-	101 nm3

	P(R)	P(R) error	Guinier	Guinier error
Forward scattering, I0	0.04249	3.4E-5	0.04245	4.2E-5
Radius of gyration, Rg	2.832 nm	0.003	2.833 nm	0.005

	Min	Max
D	-	8.7
Guinier point	1	51