Skip to main content
Log in

Robust fluorescent proteins for high-resolution microscopy and biochemical techniques

  • Research Briefing
  • Published:

From Nature Methods

View current issue Submit your manuscript

Hyperfolder yellow fluorescent protein (hfYFP) and its variants are fluorescent proteins with high chemical and thermal stability. They resist aggregation, withstand diverse chemical challenges and show promise in expansion and electron microscopies. The chloride resistance and uncanny stability in guanidinium of hfYFP enable fluorescence-guided protein purification under denaturing conditions.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1: hfYFP is useful for microscopy and biochemical techniques.

References

  1. Ueda, H. R. et al. Tissue clearing and its applications in neuroscience. Nat. Rev. Neurosci. 21, 61–79 (2020). Summary of recent tissue clearing techniques and reagents.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  2. Paez-Segala, M. G. et al. Fixation-resistant photoactivatable fluorescent proteins for CLEM. Nat. Methods 12, 215–218 (2015). Fixation-resistant mEos4b (a green-to-red photoconvertible FP from coral) for CLEM.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  3. Campbell, B. C. et al. mGreenLantern: a bright monomeric fluorescent protein with rapid expression and cell filling properties for neuronal imaging. Proc. Natl Acad. Sci. USA 117, 30710–30721 (2020). Engineering of the super-bright mGL, which led to hfYFP.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  4. Wang, Z. et al. Brain-wide analysis of the supraspinal connectome reveals anatomical correlates to functional recovery after spinal injury. eLife 11, e76254 (2022). Use of nuclearly localized mGL in 3DISCO (3D imaging of solvent-cleared organs) tissue clearing.

    Article  PubMed  PubMed Central  Google Scholar 

  5. Pédelacq, J. D. et al. Engineering and characterization of a superfolder green fluorescent protein. Nat. Biotechnol. 24, 79–88 (2006). Engineering of superfolder GFP.

    Article  PubMed  Google Scholar 

Download references

Additional information

Publisher’s note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

This is a summary of: Campbell, B. C., Paez-Segala, M. G., Looger, L. L., Petsko, G. A. & Liu, C. F. Chemically stable fluorescent proteins for advanced microscopy. Nat. Methods https://doi.org/10.1038/s41592-022-01660-7 (2022).

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Robust fluorescent proteins for high-resolution microscopy and biochemical techniques. Nat Methods 19, 1534–1535 (2022). https://doi.org/10.1038/s41592-022-01661-6

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/s41592-022-01661-6

  • Springer Nature America, Inc.

Navigation