8ZXH
Structure of the red fluorescent protein mScarlet3-H at pH 4.5
Summary for 8ZXH
| Entry DOI | 10.2210/pdb8zxh/pdb |
| Descriptor | red fluorescent protein mYongHong (2 entities in total) |
| Functional Keywords | red fluorescent protein, myonghong, fluorescent protein |
| Biological source | Discosoma sp. |
| Total number of polymer chains | 1 |
| Total formula weight | 24805.04 |
| Authors | |
| Primary citation | Xiong, H.,Chang, Q.,Ding, J.,Wang, S.,Zhang, W.,Li, Y.,Wu, Y.,Lin, P.,Yang, C.,Liu, M.,Fang, G.,Yang, Y.,Xie, J.,Qi, D.,Jiang, T.,Fu, W.,Hu, F.,Chen, Y.,Yue, R.,Li, Y.,Cui, Y.,Li, M.,Fan, S.,Yang, Y.,Xu, Y.,Li, D.,Zhang, F.,Zhao, H.,Wu, C.,Zheng, Q.,Piatkevich, K.D.,Fu, Z. A highly stable monomeric red fluorescent protein for advanced microscopy. Nat.Methods, 22:1288-1298, 2025 Cited by PubMed Abstract: The stability of fluorescent proteins (FPs) is crucial for imaging techniques such as live-cell imaging, super-resolution microscopy and correlative light and electron microscopy. Although stable green and yellow FPs are available, stable monomeric red FPs (RFPs) remain limited. Here we develop an extremely stable monomeric RFP named mScarlet3-H and determine its structure at a 1.5 Å resolution. mScarlet3-H exhibits remarkable resistance to high temperature, chaotropic conditions and oxidative environments, enabling efficient correlative light and electron microscopy imaging and rapid (less than 1 day) whole-organ tissue clearing. In addition, its high photostability allows long-term three-dimensional structured illumination microscopy imaging of mitochondrial dynamics with minimal photobleaching. It also facilitates dual-color live-cell stimulated emission depletion imaging with a high signal-to-noise ratio and strong specificity. Systematic benchmarking against high-performing RFPs established mScarlet3-H as a highly stable RFP for multimodality microscopy in cell cultures and model organisms, complementing green FPs for multiplexed imaging in zebrafish, mice and Nicotiana benthamiana. PubMed: 40247125DOI: 10.1038/s41592-025-02676-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.46 Å) |
Structure validation
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