Abstract
The major bottleneck in macromolecular crystallography is the production of well-diffracting crystals. To increase the crystallization success, we developed a crystallization strategy customizable for each protein and tested it on selected model and in-house non-yet-crystallized proteins. The underlying concept is to use in crystallization cocktails compounds that increase the thermal stability of the protein. This customized strategy yielded not only twice as many crystal hits as the standard approach but also crystal hits for two additional proteins compared to the benchmark workflow. The inherently simple design and the modular and flexible nature of the platform makes it easy to modify, further develop, and optimize individual steps. The information gained can also be used to increase the monodispersity and stability of proteins, improving in this way their amenability for biochemical studies and eventually derive a possible function of not yet annotated proteins.
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