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bioRxiv · 10.64898/2026.02.22.707290

Towards crystal structures of filament forming proteins

Roske, Y.·Leidert, M.·Rehbein, K.·Diehl, A.
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Abstract

Filament-forming proteins such as TasA (Bacillus subtilis) and camelysins CalY1, CalY2 (Bacillus cereus) pose a particular challenge for structural analysis due to their strong tendency to self-association and their polydispersity, which severely limits their ability to crystallize or to be a target for NMR-spectroscopy. To address this, it is necessary to modify the amino acid sequence to prevent filamentation. Engineering a series of N- and C-terminal truncated variants by removing flexible parts is often key to success. N-terminal extensions are also a powerful tool for obtaining crystals of fiber-forming proteins.

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Roske, Y., Leidert, M., Rehbein, K., Diehl, A.. 2026-02-22. Towards crystal structures of filament forming proteins. https://doi.org/10.64898/2026.02.22.707290

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