8ILK
Crystal structure of a highly photostable and bright green fluorescent protein at pH8.5
Summary for 8ILK
| Entry DOI | 10.2210/pdb8ilk/pdb |
| Descriptor | Green FLUORESCENT PROTEIN, CHLORIDE ION (3 entities in total) |
| Functional Keywords | photostable, green fluorescent protein, fluorescent protein |
| Biological source | synthetic construct |
| Total number of polymer chains | 2 |
| Total formula weight | 50751.49 |
| Authors | Ago, H.,Ando, R.,Hirano, M.,Shimozono, S.,Miyawaki, A.,Yamamoto, M. (deposition date: 2023-03-03, release date: 2023-10-04, Last modification date: 2024-10-30) |
| Primary citation | Ando, R.,Shimozono, S.,Ago, H.,Takagi, M.,Sugiyama, M.,Kurokawa, H.,Hirano, M.,Niino, Y.,Ueno, G.,Ishidate, F.,Fujiwara, T.,Okada, Y.,Yamamoto, M.,Miyawaki, A. StayGold variants for molecular fusion and membrane-targeting applications. Nat.Methods, 21:648-656, 2024 Cited by PubMed Abstract: Although StayGold is a bright and highly photostable fluorescent protein, its propensity for obligate dimer formation may hinder applications in molecular fusion and membrane targeting. To attain monovalent as well as bright and photostable labeling, we engineered tandem dimers of StayGold to promote dispersibility. On the basis of the crystal structure of this fluorescent protein, we disrupted the dimerization to generate a monomeric variant that offers improved photostability and brightness compared to StayGold. We applied the new monovalent StayGold tools to live-cell imaging experiments using spinning-disk laser-scanning confocal microscopy or structured illumination microscopy. We achieved cell-wide, high-spatiotemporal resolution and sustained imaging of dynamic subcellular events, including the targeting of endogenous condensin I to mitotic chromosomes, the movement of the Golgi apparatus and its membranous derivatives along microtubule networks, the distribution of cortical filamentous actin and the remolding of cristae membranes within mobile mitochondria. PubMed: 38036853DOI: 10.1038/s41592-023-02085-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.56 Å) |
Structure validation
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