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I04-Macromolecular Crystallography	An unusual disulfide-linked dimerization in the fluorescent protein rsCherryRev1.4 Thi Yen Hang Bui , Peter Dedecker , Luc Van Meervelt Acta Crystallographica Section F Structural Biology Communications 79, 38 - 44 DOI: 10.1107/S2053230X23000572 Diamond Proposal Number(s): [19190] Show Abstract ▼ Abstract: rsCherryRev1.4 has been reported as one of the reversibly photoswitchable variants of mCherry, and is an improved version with a faster off-switching speed and lower switching fatigue at high light intensities than its precursor rsCherryRev. However, rsCherryRev1.4 still has some limitations such as a tendency to dimerize as well as complex photophysical properties. Here, the crystal structure of rsCherryRev1.4 was determined at a resolution of 2 Å and it was discovered that it forms a dimer that shows disulfide bonding between the protomers. Mutagenesis, gel electrophoresis and size-exclusion chromatography strongly implicate Cys24 in this process. Replacing Cys24 in rsCherryRev1.4 resulted in a much lower tendency towards dimerization, while introducing Cys24 into mCherry correspondingly increased its dimerization. In principle, this finding opens the possibility of developing redox sensors based on controlled dimerization via disulfide cross-linking in fluorescent proteins, even though the actual application of engineering such sensors still requires additional research.	Feb 2023
I02-Macromolecular Crystallography	Structure‐function dataset reveals environment effects within a fluorescent protein model system Elke De Zitter , Siewert Hugelier , Sam Duwé , Wim Vandenberg , Alison G. Tebo , Luc Van Meervelt , Peter Dedecker Angewandte Chemie International Edition DOI: 10.1002/anie.202015201 Show Abstract ▼ Abstract: Anisotropic environments can drastically alter the spectroscopy and photochemistry of molecules, leading to complex structure‐function relationships. We examined this using fluorescent proteins as easy‐to‐modify model systems. Starting from a single scaffold, we have developed a range of 27 photochromic fluorescent proteins that cover a broad range of spectroscopic properties, including the determination of 43 crystal structures. Correlation and principal component analysis confirmed the complex relationship between structure and spectroscopy, but also allowed us to identify consistent trends and to relate these to the spatial organization. We find that changes in spectroscopic properties can come about through multiple underlying mechanisms, of which polarity, hydrogen bonding and presence of water molecules are key modulators. We anticipate that our findings and rich structure/spectroscopy dataset can open opportunities for the development and evaluation of new and existing protein engineering methods.	Feb 2021

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