Protein crystallization plays a vital role in structural biology and in structure guided drug design in the pharmaceutical industry. Despite significant efforts aimed at improving the productivity of crystallization in structural biology pipelines, the average success rate for isolating X-ray diffraction quality protein crystals in most labs remains in the 15-20% range. Systematic manipulation of the surface energy of the crystallization substrate or container surface can reduce the energetic barriers to crystal nucleation, and DeNovX achieves this using engineered nucleation features (ENFs) that improve crystallization outcomes for proteins and small molecules. Survey studies of six proteins using six different ENFs have reproducibly demonstrated an average 3-fold increase in hit percentages and production of 2.5-fold more crystalline material in 40% less time with preservation of the X-ray diffraction structure quality. In addition to these functional survey results, replicate and quantitative measurements of temperature variation studies of lysozyme crystallization using a grid-based ENF vs. control surfaces will be presented, as will the results of contact angle and surface energy measurements.

Use of engineered nucleation features for improved protein crystallization

ACS Spring Meeting 2021

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