11MQ
Crystal Structure of Fluorophore-binding Protein NovoTag657-holo
This is a non-PDB format compatible entry.
Summary for 11MQ
| Entry DOI | 10.2210/pdb11mq/pdb |
| Descriptor | NovoTag657-holo, SULFATE ION, ZINC ION, ... (5 entities in total) |
| Functional Keywords | de novo designed protein, small molecule binder, fluorophore-binding, de novo protein, multiplex imaging |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 16820.11 |
| Authors | Bera, A.K.,Tran, L.,An, L.,Kang, A.,Baker, D. (deposition date: 2026-03-05, release date: 2026-07-22, Last modification date: 2026-07-29) |
| Primary citation | Tran, L.,Klein, S.,Juergens, D.,Sharma, S.,Decarreau, J.,Lee, G.R.,Wang, Y.,Chen, W.,Bera, A.K.,Kang, A.,Woods, J.,Joyce, E.,Vafeados, D.K.,Roullier, N.,Li, X.,Liu, B.,Bo, Y.,Muratspahic, E.,Brown, T.A.,Grimm, J.B.,Patel, R.,Lavis, L.D.,Mahamid, J.,An, L.,Baker, D. De novo design of orthogonal far-red, orange, and green fluorophore-binding proteins for multiplexed imaging. Science, :eaeb0822-eaeb0822, 2026 Cited by PubMed Abstract: Fluorescent proteins and small-molecule dyes offer complementary advantages for biological imaging: proteins are amenable to genetic tagging, whereas dyes provide superior brightness and photostability. To combine these strengths, we used de novo protein design to generate small, nanomolar-affinity, high-selectivity binders (NovoTags) for three cell-permeable dyes spanning the visible spectrum. We show that the NovoTag fluorescent lifetimes can be tuned and demonstrate their application in lifetime and wavelength-based multiplexed fluorescence imaging. We further design a two-chain NovoTag that functions as a chemically induced dimerization system with fluorescent readout in living cells, or as a minimally perturbing proximity probe in fixed cells. Our approach combines the advantages of fluorescent proteins and small-molecule dyes, expanding the toolkit for cellular imaging. PubMed: 42461986DOI: 10.1126/science.aeb0822 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.38 Å) |
Structure validation
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