The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Structure-guided evolution of cyan fluorescent proteins towards a quantum yield of 93%
Open accessAbstract
Cyan variants of green fluorescent protein are widely used as donors in Förster resonance energy transfer experiments. The popular, but modestly bright, Enhanced Cyan Fluorescent Protein (ECFP) was sequentially improved into the brighter variants Super Cyan Fluorescent Protein 3A (SCFP3A) and mTurquoise, the latter exhibiting a high-fluorescence quantum yield and a long mono-exponential fluorescence lifetime. Here we combine X-ray crystallography and excited-state calculations to rationalize these stepwise improvements. The enhancement originates from stabilization of the seventh β-strand and the strengthening of the sole chromophore-stabilizing hydrogen bond. The structural analysis highlighted one suboptimal internal residue, which was subjected to saturation mutagenesis combined with fluorescence lifetime-based screening. This resulted in mTurquoise2, a brighter variant with faster maturation, high photostability, longer mono-exponential lifetime and the highest quantum yield measured for a monomeric fluorescent protein. Together, these properties make mTurquoise2 the preferable cyan variant of green fluorescent protein for long-term imaging and as donor for Förster resonance energy transfer to a yellow fluorescent protein.
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Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
The CCP4 suite: programs for protein crystallography
Collaborative Computational Project, N. 4. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,270
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463
Jorgensen, W. L., Maxwell, D. S., & Tirado-Rives, J. (1996) · Journal of the American Chemical Society · doi:10.1021/ja9621760 · Cited by 15,409
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,742
Tsien, R. Y. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.509 · Cited by 6,143
A guide to choosing fluorescent proteins
Shaner, N. C., Steinbach, P. A., & Tsien, R. Y. (2005) · Nature Methods · doi:10.1038/nmeth819 · Cited by 2,840
Nagai, T., Ibata, K., Park, E. S., Kubota, M., Mikoshiba, K., & Miyawaki, A. (2002) · Nature Biotechnology · doi:10.1038/nbt0102-87 · Cited by 2,753
Crystal Structure of the Aequorea victoria Green Fluorescent Protein
Ormö, M., Cubitt, A. B., Kallio, K., Gross, L. A., Tsien, R. Y., & Remington, S. J. (1996) · Science · doi:10.1126/science.273.5280.1392 · Cited by 2,242
Partitioning of Lipid-Modified Monomeric GFPs into Membrane Microdomains of Live Cells
Zacharias, D. A., Violin, J. D., Newton, A. C., & Tsien, R. Y. (2002) · Science · doi:10.1126/science.1068539 · Cited by 2,235
Cited by
Chan, K. Y., Jang, M. J., Yoo, B. B., Greenbaum, A., Ravi, N., Wu, W.-L., Sánchez-Guardado, L., Lois, C., Mazmanian, S. K., Deverman, B. E., et al. (2017) · Nature Neuroscience · doi:10.1038/nn.4593 · Cited by 1,578
Improving FRET dynamic range with bright green and red fluorescent proteins
Lam, A. J., St-Pierre, F., Gong, Y., Marshall, J. D., Cranfill, P. J., Baird, M. A., McKeown, M. R., Wiedenmann, J., Davidson, M. W., Schnitzer, M. J., et al. (2012) · Nature Methods · doi:10.1038/nmeth.2171 · Cited by 732
A novel probe for phosphatidylinositol 4-phosphate reveals multiple pools beyond the Golgi
Hammond, G. R. V., Machner, M. P., & Balla, T. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201312072 · Cited by 453
Repeated ER–endosome contacts promote endosome translocation and neurite outgrowth
Raiborg, C., Wenzel, E. M., Pedersen, N. M., Olsvik, H., Schink, K. O., Schultz, S. W., Vietri, M., Nisi, V., Bucci, C., Brech, A., et al. (2015) · Nature · doi:10.1038/nature14359 · Cited by 414
Bajar, B. T., Wang, E. S., Lam, A. J., Kim, B. B., Jacobs, C. L., Howe, E. S., Davidson, M. W., Lin, M. Z., & Chu, J. (2016) · Scientific Reports · doi:10.1038/srep20889 · Cited by 389
Metadata
- Authors
- Goedhart, J., von Stetten, D., Noirclerc-Savoye, M., Lelimousin, M., Joosen, L., Hink, M. A., van Weeren, L., Gadella, T. W. J., & Royant, A.
- Venue
- Nature Communications
- Published
- 2012-03-20
- Volume
- 3
- Issue
- 1
- Pages
- 751-751
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2168080864
- Cited by
- 787
- References
- 35
- FWCI
- 20.38
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Goedhart, J., von Stetten, D., Noirclerc-Savoye, M., Lelimousin, M., Joosen, L., Hink, M. A., van Weeren, L., Gadella, T. W. J., & Royant, A. (2012). Structure-guided evolution of cyan fluorescent proteins towards a quantum yield of 93%. Nature Communications. https://doi.org/10.1038/ncomms1738
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