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A multilaboratory comparison of calibration accuracy and the performance of external references in analytical ultracentrifugation
H. Zhao, R. Ghirlando, C. Alfonso, F. Arisaka, I. Attali, DL. Bain, MM. Bakhtina, DF. Becker, GJ. Bedwell, A. Bekdemir, TM. Besong, C. Birck, CA. Brautigam, W. Brennerman, O. Byron, A. Bzowska, JB. Chaires, CT. Chaton, H. Cölfen, KD. Connaghan,...
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, Research Support, N.I.H., Extramural, práce podpořená grantem
NLK
Directory of Open Access Journals
od 2006
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od 2006
Public Library of Science (PLoS)
od 2006
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od 2006
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od 2006-12-01
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od 2006-01-01
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od 2006-10-01
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od 2006-01-01
Medline Complete (EBSCOhost)
od 2008-01-01
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od 2006-12-01
Health & Medicine (ProQuest)
od 2006-12-01
Public Health Database (ProQuest)
od 2006-12-01
ROAD: Directory of Open Access Scholarly Resources
od 2006
- MeSH
- kalibrace MeSH
- reprodukovatelnost výsledků MeSH
- ultracentrifugace metody normy MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Research Support, N.I.H., Extramural MeSH
Analytical ultracentrifugation (AUC) is a first principles based method to determine absolute sedimentation coefficients and buoyant molar masses of macromolecules and their complexes, reporting on their size and shape in free solution. The purpose of this multi-laboratory study was to establish the precision and accuracy of basic data dimensions in AUC and validate previously proposed calibration techniques. Three kits of AUC cell assemblies containing radial and temperature calibration tools and a bovine serum albumin (BSA) reference sample were shared among 67 laboratories, generating 129 comprehensive data sets. These allowed for an assessment of many parameters of instrument performance, including accuracy of the reported scan time after the start of centrifugation, the accuracy of the temperature calibration, and the accuracy of the radial magnification. The range of sedimentation coefficients obtained for BSA monomer in different instruments and using different optical systems was from 3.655 S to 4.949 S, with a mean and standard deviation of (4.304 ± 0.188) S (4.4%). After the combined application of correction factors derived from the external calibration references for elapsed time, scan velocity, temperature, and radial magnification, the range of s-values was reduced 7-fold with a mean of 4.325 S and a 6-fold reduced standard deviation of ± 0.030 S (0.7%). In addition, the large data set provided an opportunity to determine the instrument-to-instrument variation of the absolute radial positions reported in the scan files, the precision of photometric or refractometric signal magnitudes, and the precision of the calculated apparent molar mass of BSA monomer and the fraction of BSA dimers. These results highlight the necessity and effectiveness of independent calibration of basic AUC data dimensions for reliable quantitative studies.
Beckman Coulter Inc Life Science Division Indianapolis Indiana 46268 United States of America
Biochemistry Core Facility Max Planck Institute of Biochemistry 82152 Martinsried Germany
Biochemistry Department University of Cambridge Cambridge CB2 1GA United Kingdom
Biophysics Core Facility Scientific Instrument Center Academia Sinica Taipei 115 Taiwan
Biophysics of Macromolecules German Cancer Research Center Heidelberg 69120 Germany
CEA IBS F 38044 Grenoble France
Central Instrument Center Mokpo National University Muan 534 729 Korea
CNRS IBS F 38044 Grenoble France
Core Facility International Institute of Molecular and Cell Biology Warsaw 02 109 Poland
Department of Biochemistry and Molecular Biology Tel Aviv University Tel Aviv 69978 Israel
Department of Biology Haverford College Haverford Pennsylvania 19041 United States of America
Department of Chemistry and Biochemistry Concordia University Montreal Quebec H4B 1R6 Canada
Department of Chemistry Mokpo National University Muan 534 729 Korea
Department of Physical Chemistry University of Murcia Murcia 30071 Spain
Diabetes Biophysics Novo Nordisk A S Måløv 2760 Denmark
Enzyme Research Group Concordia University Montreal Quebec H4B 1R6 Canada
ICS 6 Structural Biochemistry Research Center Juelich 52428 Juelich Germany
Institut Pasteur Centre of Biophysics of Macromolecules and Their Interactions Paris 75724 France
Institute for Biophysical Chemistry Hannover Medical School 30625 Hannover Germany
Institute of Biological Chemistry Academia Sinica Taipei 115 Taiwan
JG Brown Cancer Center University of Louisville Louisville Kentucky 40202 United States of America
Life Science Research Center Nihon University College of Bioresource Science Fujisawa 252 0880 Japan
Molecular Biophysics Suite Department of Biochemistry Oxford Oxon OX1 3QU United Kingdom
Physical Chemistry University of Konstanz 78457 Konstanz Germany
Proteome and Protein Analysis University of Newcastle Newcastle upon Tyne NE1 7RU United Kingdom
Redox Biology Center University of Nebraska Lincoln Lincoln Nebraska 68588 United States of America
Research Complex at Harwell Rutherford Appleton Laboratory Oxfordshire OX11 0FA United Kingdom
Rudolf Virchow Center for Experimental Biomedicine University of Würzburg 97080 Würzburg Germany
School of Life Sciences University of Glasgow Glasgow G37TT United Kingdom
Structural Biology Platform IGBMC Illkirch 67400 France
Technology Facility Department of Biology University of York York YO10 5DD United Kingdom
Univ Grenoble Alpes IBS F 38044 Grenoble France
Wadsworth Center New York State Department of Health Albany New York 12208 United States of America
Citace poskytuje Crossref.org
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- $a Analytical ultracentrifugation (AUC) is a first principles based method to determine absolute sedimentation coefficients and buoyant molar masses of macromolecules and their complexes, reporting on their size and shape in free solution. The purpose of this multi-laboratory study was to establish the precision and accuracy of basic data dimensions in AUC and validate previously proposed calibration techniques. Three kits of AUC cell assemblies containing radial and temperature calibration tools and a bovine serum albumin (BSA) reference sample were shared among 67 laboratories, generating 129 comprehensive data sets. These allowed for an assessment of many parameters of instrument performance, including accuracy of the reported scan time after the start of centrifugation, the accuracy of the temperature calibration, and the accuracy of the radial magnification. The range of sedimentation coefficients obtained for BSA monomer in different instruments and using different optical systems was from 3.655 S to 4.949 S, with a mean and standard deviation of (4.304 ± 0.188) S (4.4%). After the combined application of correction factors derived from the external calibration references for elapsed time, scan velocity, temperature, and radial magnification, the range of s-values was reduced 7-fold with a mean of 4.325 S and a 6-fold reduced standard deviation of ± 0.030 S (0.7%). In addition, the large data set provided an opportunity to determine the instrument-to-instrument variation of the absolute radial positions reported in the scan files, the precision of photometric or refractometric signal magnitudes, and the precision of the calculated apparent molar mass of BSA monomer and the fraction of BSA dimers. These results highlight the necessity and effectiveness of independent calibration of basic AUC data dimensions for reliable quantitative studies.
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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- 700 1_
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