Evidence map›Paper›PMID 15263848›Full record

ArticleJournal of structural and functional genomics2004

Production of selenomethionine-labeled proteins in two-liter plastic bottles for structure determination.

Lucy Stols, Cynthia Sanville Millard, Irina Dementieva, Mark I Donnelly

Abstract read
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In one paragraph

Article in Journal of structural and functional genomics, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
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  3. Article
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  5. Article
  6. Article
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  9. Article
  10. Current strategies for protein production and purification enabling membrane protein structural biology.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2016
    Review
  11. Article
  12. New aminopeptidase from "microbial dark matter" archaeon.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015
    Article
  13. Article
  14. Article
  15. Protein production for structural genomics using E. coli expression.Methods in molecular biology (Clifton, N.J.) · 2014
    Article
  16. Article
  17. Review
  18. Article
  19. Cleavable C-terminal His-tag vectors for structure determination.Journal of structural and functional genomics · 2010
    Article
  20. Crystallization and preliminary X-ray diffraction studies of FAD synthetase from Corynebacterium ammoniagenes.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009
    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

4 authors.

Lucy StolsEnvironmental Research Division, Argonne National Laboratory, Argonne, IL 60439, USA.
Cynthia Sanville Millard
Irina Dementieva
Mark I Donnelly

Funding

THE MIDWEST CENTER FOR STRUCTURAL GENOMICSP50GM062414 · NIGMS · UNIVERSITY OF CHICAGO · PI JOACHIMIAK, ANDRZEJ JOACHIMIAK · 2000 to 2004
$33.2M
NIGMS NIH HHS GM62414-01
6 · The paper itself

Abstract

A simplified approach developed recently for the production of heterologous proteins in Escherichia coli uses 2-liter polyethylene terephthalate beverage bottles as disposable culture vessels [Sanville Millard, C. et al. 2003. Protein Expr. Purif. 29, 311-320]. The method greatly reduces the time and effort needed to produce native proteins for structural or functional studies. We now demonstrate that the approach is also well suited for production of proteins in defined media with incorporation of selenomethionine to facilitate structure determination by multiwavelength anomalous diffraction. Induction of a random set of Bacillus stearothermophilus target genes under the new protocols generated soluble selenomethionyl proteins in good yield. Several selenomethionyl proteins were purified in good yields and three were subjected to amino acid analysis. Incorporation of selenomethionine was determined to be greater than 95% in one protein and greater than 98% in the other two. In the preceding paper [Zhao et al., this issue, pp. 87-93], the approach is further extended to production of [U-15N]- or [U-13C, U-15N]-labeled proteins. The approach thus appears suitable for high-throughput production of proteins for structure determination by X-ray crystallography or nuclear magnetic resonance spectroscopy.

Indexed as

Bacterial ProteinsCarbon IsotopesEscherichia coliGenes, BacterialGeobacillus stearothermophilusMolecular StructureNitrogen IsotopesPolyethylene TerephthalatesProteomicsRecombinant ProteinsSelenomethionineBacterial ProteinsCarbon IsotopesNitrogen IsotopesPolyethylene TerephthalatesRecombinant ProteinsSelenomethionine

Identifiers

What OpenQuestion holds

Textmetadata
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.