ArticleJournal of structural and functional genomics2004
Production in two-liter beverage bottles of proteins for NMR structure determination labeled with either 15N- or 13C-15N.
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 15 papers.
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Who cites it
15 citing papers in PubMed, 22 citations in OpenAlex.
- Cost-effective large-scale expression of proteins for NMR studies.Journal of biomolecular NMR · 2018Article
- Protein stability: a crystallographer's perspective.Acta crystallographica. Section F, Structural biology communications · 2016Review
- Solution Structural Studies of GTP:Adenosylcobinamide-Phosphateguanylyl Transferase (CobY) from Methanocaldococcus jannaschii.PloS one · 2015Article
- Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU).The Journal of biological chemistry · 2013Article
- High throughput platforms for structural genomics of integral membrane proteins.Current opinion in structural biology · 2011Review
- Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.Methods in enzymology · 2011Article
- Decimal place slope, a fast and precise method for quantifying 13C incorporation levels for detecting the metabolic activity of microbial species.Molecular & cellular proteomics : MCP · 2010Article
- Solution structure of the iron-sulfur cluster cochaperone HscB and its binding surface for the iron-sulfur assembly scaffold protein IscU.Biochemistry · 2008Article
- Chapter 3. High-throughput protein purification for x-ray crystallography and NMR.Advances in protein chemistry and structural biology · 2008Review
- Functional protein expression from a DNA based wheat germ cell-free system.Journal of structural and functional genomics · 2007Article
- Structures of proteins of biomedical interest from the Center for Eukaryotic Structural Genomics.Journal of structural and functional genomics · 2007Review
- Three-dimensional structure determined for a subunit of human tRNA splicing endonuclease (Sen15) reveals a novel dimeric fold.Journal of molecular biology · 2007Article
- Micelle-induced folding of spinach thylakoid soluble phosphoprotein of 9 kDa and its functional implications.Biochemistry · 2006Article
- Solution structure of a calmodulin-like calcium-binding domain from Arabidopsis thaliana.Journal of biomolecular NMR · 2004Article
- Production of selenomethionine-labeled proteins in two-liter plastic bottles for structure determination.Journal of structural and functional genomics · 2004Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
The use of 2-L polyethylene terephthalate beverage bottles as a bacterial culture vessel has been recently introduced as an enabling technology for high-throughput structural biology [Sanville Millard, C. et al., 2003. Protein Express. Purif. 29, 311-320]. In the article following this one [Stols et al., this issue, pp. 95-102], this approach was elaborated for selenomethionine labeling used for multiwavelength anomalous dispersion phasing in the X-ray crystallographic determinations of protein structure. Herein, we report an effective and reproducible schedule for uniform 15N- and 13C-labeling of recombinant proteins in 2-L beverage bottles for structural determination by NMR spectroscopy. As an example, three target proteins selected from Arabidopsis thaliana were expressed in Escherichia coli Rosetta (DE3)/pLysS from a T7-based expression vector, purified, and characterized by electrospray ionization mass spectrometry and NMR analysis by 1H-15N heteronuclear single quantum correlation spectroscopy. The results show that expressions in the unlabeled medium provide a suitable control for estimation of the level of production of the labeled protein. Mass spectral characterizations show that the purified proteins contained a level of isotopic incorporation equivalent to the isotopically labeled materials initially present in the growth medium, while NMR analysis of the [U-15N]-labeled proteins provided a convenient method to assess the solution state properties of the target protein prior to production of a more costly double-labeled sample.
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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.