The crystallization of proteins, nucleic acids, biological complexes, will depend on the creation of a solution that is supersaturated in the macromolecule. Since 60 years, X-ray crystallography provides structural details of protein molecules, information that is crucial to unravel biological mechanisms at molecular level. Crystallography requires that sample is in crystal form. Getting such crystals at an acceptable quality for crystallographic analysis is not trivial and strategies to make this process less expensive and time-consuming are not available, still now.
Technologies that assist with Protein crystallization
- High throughput crystallization screening
- Protein engineering
Advanced materials represent a turning point in this field because they can be exploited to control nucleation and growth step making more effective the crystallization process. Researchers are developing membrane-based materials able to trigger protein crystallization also in conditions that are not fruitful by standard methods. Such materials have a great impact both in the industry and academic studies because significantly reduce cost and time of the protein purification and crystallization process. Then they developed membrane-materials functionalized by hydrogel that proved ability in getting very stress-resistant crystals, which are suitable for structure-based drug design studies that require very harsh soaking conditions. This material, similarly to our metal oxide nanoparticle-functionalized membrane, significantly widens the crystallization window and produce crystals having good diffraction quality.
Methods of protein crystallization
- Vapor diffusion
- Free-interface diffusion
Membrane-based materials are showing very effective in protein crystallization and to produce crystals having specific features. Our efforts are focusing now in functionalizing such materials by Nano template to crystallize very challenging proteins such as intact antibodies, and to develop membrane able to promote bio mineralization and to enable polymorphs selection.