ArticleMethods in enzymology2019
Sortase-mediated fluorescent labeling of CRISPR complexes.
Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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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.
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Who cites it
3 citing papers in PubMed.
- Site-Specific C-Terminal Fluorescent Labeling of Tau Protein.ACS omega · 2022Article
- Polymerase theta-helicase promotes end joining by stripping single-stranded DNA-binding proteins and bridging DNA ends.Nucleic acids research · 2022Article
- Inexpensive robotic system for standard and fluorescent imaging of protein crystals.Acta crystallographica. Section F, Structural biology communications · 2019Article
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Authors and funding
10 authors.
Funding
Abstract
Fluorescent labeling of proteins is a critical requirement for single-molecule imaging studies. Many protein labeling strategies require harsh conditions or large epitopes that can inactivate the target protein, either by decreasing the protein's enzymatic activity or by blocking protein-protein interactions. Here, we provide a detailed protocol to efficiently label CRISPR-Cas complexes with a small fluorescent peptide via sortase-mediated transpeptidation. The sortase tag consists of just a few amino acids that are specifically recognized at either the N- or the C-terminus, making this strategy advantageous when the protein is part of a larger complex. Sortase is active at high ionic strength, 4°C, and with a broad range of organic fluorophores. We discuss the design, optimization, and single-molecule fluorescent imaging of CRISPR-Cas complexes on DNA curtains. Sortase-mediated transpeptidation is a versatile addition to the protein labeling toolkit.
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