ArticleProtein science : a publication of the Protein Society2008
Thioredoxin as a fusion tag for carrier-driven crystallization.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Combinatorial protein engineering identifies potent CRISPR activators with reduced toxicity.Nature communications · 2025Article
- Tagging Recombinant Proteins to Enhance Solubility and Aid Purification.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Overcoming the Solubility Problem in E. coli: Available Approaches for Recombinant Protein Production.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Identification of phenothiazine derivatives as UHM-binding inhibitors of early spliceosome assembly.Nature communications · 2020Article
- The Effect of Recombinant Tags onPlants (Basel, Switzerland) · 2020Article
- HuR biological function involves RRM3-mediated dimerization and RNA binding by all three RRMs.Nucleic acids research · 2019Article
- T4 lysozyme-facilitated crystallization of the human molybdenum cofactor-dependent enzyme mARC.Acta crystallographica. Section F, Structural biology communications · 2018Article
- The macro domain as fusion tag for carrier-driven crystallization.Protein science : a publication of the Protein Society · 2017Article
- Interaction network of the ribosome assembly machinery from a eukaryotic thermophile.Protein science : a publication of the Protein Society · 2017Article
- Design of an expression system to enhance MBP-mediated crystallization.Scientific reports · 2017Article
- The "Sticky Patch" Model of Crystallization and Modification of Proteins for Enhanced Crystallizability.Methods in molecular biology (Clifton, N.J.) · 2017Review
- Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction.Nature communications · 2015Article
- A Suite of Engineered GFP Molecules for Oligomeric Scaffolding.Structure (London, England : 1993) · 2015Article
- Cloning, expression, crystallization and preliminary X-ray studies of a superfolder GFP fusion of cyanobacterial Psb32.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Mechanistic strategies for catalysis adopted by evolutionary distinct family 43 arabinanases.The Journal of biological chemistry · 2014Article
- Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system.Frontiers in microbiology · 2014Review
- To fuse or not to fuse: what is your purpose?Protein science : a publication of the Protein Society · 2013Review
- Application of protein engineering to enhance crystallizability and improve crystal properties.Acta crystallographica. Section D, Biological crystallography · 2010Article
- A synergistic approach to protein crystallization: combination of a fixed-arm carrier with surface entropy reduction.Protein science : a publication of the Protein Society · 2010Review
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5 authors.
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Abstract
Structural investigations are frequently hindered by difficulties in obtaining diffracting crystals of the target protein. Here, we report the crystallization and structure solution of the U2AF homology motif (UHM) domain of splicing factor Puf60 fused to Escherichia coli thioredoxin A. Both modules make extensive crystallographic contacts, contributing to a well-defined crystal lattice with clear electron density for both the thioredoxin and the Puf60-UHM module. We compare two short linker sequences between the two fusion domains, GSAM and GSPPM, for which only the GSAM-linked fusion protein yielded diffracting crystals. While specific interdomain contacts are not observed for both fusion proteins, NMR relaxation data in solution indicate reduced interdomain mobility between the Trx and Puf60-UHM modules. The GSPPM-linked fusion protein is significantly more flexible, albeit both linker sequences have the same number of degrees of torsional freedom. Our analysis provides a rationale for the crystallization of the GSAM-linked fusion protein and indicates that in this case, a four-residue linker between thioredoxin A and the fused target may represent the maximal length for crystallization purposes. Our data provide an experimental basis for the rational design of linker sequences in carrier-driven crystallization and identify thioredoxin A as a powerful fusion partner that can aid crystallization of difficult targets.
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