Evidence map›Paper›PMID 21925267›Full record

ArticleMethods (San Diego, Calif.)2011

A rapid and robust method for selective isotope labeling of proteins.

Myat T Lin, Lindsay J Sperling, Heather L Frericks Schmidt, Ming Tang, Rimma I Samoilova, Takashi Kumasaka, Toshio Iwasaki, Sergei A Dikanov, Chad M Rienstra, Robert B Gennis

Abstract read
In one paragraph

Article in Methods (San Diego, Calif.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.2field-weighted citation impact, top 8% of its field
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

29 citing papers in PubMed, 74 citations in OpenAlex.

  1. Optimized histidine-specific isotopic labeling in proteins overproduced in Escherichia coli.Protein science : a publication of the Protein Society · 2026
    Article
  2. Article
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  10. Extensively sparseJournal of biomolecular NMR · 2021
    Article
  11. Review
  12. Capturing Peptide-GPCR Interactions and Their Dynamics.Molecules (Basel, Switzerland) · 2020
    Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Trifluoroselenomethionine: A New Unnatural Amino Acid.Chembiochem : a European journal of chemical biology · 2016
    Article
  19. Article
  20. Review
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

10 authors at 4 institutions in 3 countries.

Myat T LinDepartment of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, United States.
Lindsay J Sperling
Heather L Frericks Schmidt
Ming Tang
Rimma I Samoilova
Takashi Kumasaka
Toshio Iwasaki
Sergei A Dikanov
Chad M Rienstra
Robert B Gennis
University of Illinois Urbana-Champaign · USInstitute of Chemical Kinetics and Combustion · RUJapan Synchrotron Radiation Research Institute · JPNippon Medical School · JP

Funding

INSTITUTIONAL NRSA IN MOLECULAR BIOPHYSICST32GM008276 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GROSMAN, CLAUDIO F · 1988 to 2013
$4.8M
Structure of reaction intermediates in the bc1 complexR01GM062954 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI DIKANOV, SERGEI A · 2002 to 2010
$2.2M
Structure and Function of Membrane Protein Complexes(RMI)R01GM075937 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI RIENSTRA, CHAD M · 2005 to 2009
$1.4M
NIGMS NIH HHS 5 T32 GM008276NIGMS NIH HHS GM062954NIGMS NIH HHS R01 GM062954NIGMS NIH HHS R01 GM075937NIGMS NIH HHS R01GM075937NIGMS NIH HHS T32 GM008276
6 · The paper itself

Abstract

Amino-acid selective isotope labeling of proteins offers numerous advantages in mechanistic studies by revealing structural and functional information unattainable from a crystallographic approach. However, efficient labeling of proteins with selected amino acids necessitates auxotrophic hosts, which are often not available. We have constructed a set of auxotrophs in a commonly used Escherichia coli expression strain C43(DE3), a derivative of E. coli BL21(DE3), which can be used for isotopic labeling of individual amino acids or sets of amino acids. These strains have general applicability to either soluble or membrane proteins that can be expressed in E. coli. We present examples in which proteins are selectively labeled with (13)C- and (15)N-amino acids and studied using magic-angle spinning solid-state NMR and pulsed EPR, demonstrating the utility of these strains for biophysical characterization of membrane proteins, radical-generating enzymes and metalloproteins.

Indexed as

Amino Acid MotifsBinding SitesElectron Spin Resonance SpectroscopyElectron Transport Complex IVEscherichia coliEscherichia coli ProteinsFerredoxinsHydrogen BondingIronIsotope LabelingMembrane ProteinsModels, MolecularNuclear Magnetic Resonance, BiomolecularOrganisms, Genetically ModifiedOxidation-ReductionProtein SubunitsCyoA protein, E coliElectron Transport Complex IVEscherichia coli ProteinsFerredoxinsIronMembrane ProteinsProtein SubunitsRecombinant ProteinsSulfur

Identifiers

PMID21925267
PMCPMC3261321
OpenAlexW2048775155

What OpenQuestion holds

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LicenceTDM
Read underepoch 390

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.