Evidence map›Paper›PMID 23711724›Full record

ArticleAnalytical biochemistry2013

Improving the thermal, radial, and temporal accuracy of the analytical ultracentrifuge through external references.

Rodolfo Ghirlando, Andrea Balbo, Grzegorz Piszczek, Patrick H Brown, Marc S Lewis, Chad A Brautigam, Peter Schuck, Huaying Zhao

Abstract read
In one paragraph

Article in Analytical biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

50 citing papers in PubMed.

  1. Article
  2. Article
  3. Evolution of a fuzzy ribonucleoprotein complex in viral assembly.bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Assembly reactions of SARS-CoV-2 nucleocapsid protein with nucleic acid.bioRxiv : the preprint server for biology · 2023
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Calibrating analytical ultracentrifuges.European biophysics journal : EBJ · 2021
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Nucleic acid-induced dimerization of HIV-1 Gag protein.The Journal of biological chemistry · 2019
    Article
  20. Cryo-EM structure of substrate-freeCurrent research in structural biology · 2019
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Rodolfo GhirlandoLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Andrea Balbo
Grzegorz Piszczek
Patrick H Brown
Marc S Lewis
Chad A Brautigam
Peter Schuck
Huaying Zhao

Funding

Biophysics FacilityZICHL000338 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI PISZCZEK, GRZEGORZ · 2009 to 2025
$12.2M
Dynamics of Protein Assemblies by Analytical UltracentrifugationZIAEB000051 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI SCHUCK, PETER · 2009 to 2025
$7.9M
Biophysics of Macromolecular ComplexesZIADK033007 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2024
$4.9M
Quantitative Methods for Macromolecular InteractionsZICEB000079 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI BALBO, ANDREA · 2011 to 2015
$1.0M
Intramural NIH HHS ZIA EB000051
6 · The paper itself

Abstract

Sedimentation velocity (SV) is a method based on first principles that provides a precise hydrodynamic characterization of macromolecules in solution. Due to recent improvements in data analysis, the accuracy of experimental SV data emerges as a limiting factor in its interpretation. Our goal was to unravel the sources of experimental error and develop improved calibration procedures. We implemented the use of a Thermochron iButton temperature logger to directly measure the temperature of a spinning rotor and detected deviations that can translate into an error of as much as 10% in the sedimentation coefficient. We further designed a precision mask with equidistant markers to correct for instrumental errors in the radial calibration that were observed to span a range of 8.6%. The need for an independent time calibration emerged with use of the current data acquisition software (Zhao et al., Anal. Biochem., 437 (2013) 104-108), and we now show that smaller but significant time errors of up to 2% also occur with earlier versions. After application of these calibration corrections, the sedimentation coefficients obtained from 11 instruments displayed a significantly reduced standard deviation of approximately 0.7%. This study demonstrates the need for external calibration procedures and regular control experiments with a sedimentation coefficient standard.

Indexed as

Area Under CurveCalibrationReproducibility of ResultsSerum Albumin, BovineTemperatureTimeUltracentrifugationSerum Albumin, BovineHydrodynamic modelingSedimentation equilibriumSedimentation velocity

Identifiers

PMID23711724
PMCPMC3826449

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.