X-ray crystallography remains a benchmark technique for protein structure determination complementing NMR and cryo-electron microscopy. Improvements in crystallization are needed given the low average success rates of &lt;15%, and DeNovX’s approach uses engineered modifications to the surfaces in contact with the protein solution to facilitate crystal nucleation. Replicate studies of four proteins (e.g., lysozyme, BPT, etc.) on engineered nucleation surfaces gave an average 30% reduction in crystallization onset times vs. controls, with preservation of diffraction quality. Controlled studies are underway with more challenging proteins, including one of the two component sensor histidine kinases of the opportunistic pathogen <i>Pseudomonas aeruginosa</i> (PA01), for which the crystallization hits improved 8.4-fold with crystallization onset in 87% less time when using engineered nucleation features. Systematically tuning the surface energy of the substrate or vessel in contact with the solute to be crystallized can improve crystallization outcomes while requiring minimal changes to crystallization protocols.

Improving protein crystallization outcomes using surface energy modified substrates

2019 Spring National Meeting

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