Protein structure determination remains a critical facet of understanding cellular functions and developing treatments for disease, and macromolecular X-ray crystallography is still the benchmark method for determining these structures at atomic resolution. However, time- and sample-consuming bottlenecks in the processes between final protein purification and crystallization still exist. Despite advances in high throughput crystallization workflows, &lt; 20% of crystallization screens produce positive results, and fewer crystals from these positive outcomes are of diffraction quality. DeNovX develops crystallization platforms that utilize surface energy modifications to improve crystallization outcomes while retaining diffraction quality of the crystals. Overall, we have demonstrated 1.1-8.7-fold increases in crystallization hit percentages while reducing time to crystallization by an average of 40% for a group of benchmark proteins (e.g., lysozyme, BPT, etc.) and proteins with less characterized crystallization behavior. In addition, samples prepared using engineered nucleation features generate an average of 2.5-fold more crystalline material, which is beneficial where protein supplies are limited and for emerging techniques like X-ray Free Electron Laser Serial Femtosecond Crystallography, which are acutely sample-destructive and can require hundreds or more crystals per study.

Enhancing protein crystallization screening results using engineered nucleation features

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.