Molecular nucleation mechanisms and control strategies for crystal polymorph selection

Molecular nucleation mechanisms and control strategies for crystal polymorph selection Nature 556, 7699 (2018). doi:10.1038/nature25971 Authors: Alexander E. S. Van Driessche, Nani Van Gerven, Paul H. H. Bomans, Rick R. M. Joosten, Heiner Friedrich, David Gil-Carton, Nico A. J. M. Sommerdijk & Mike Sleutel The formation of condensed (compacted) protein phases is associated with a wide range of human disorders, such as eye cataracts, amyotrophic lateral sclerosis, sickle cell anaemia and Alzheimer’s disease. However, condensed protein phases have their uses: as crystals, they are harnessed by structural biologists to elucidate protein structures, or are used as delivery vehicles for pharmaceutical applications. The physiochemical properties of crystals can vary substantially between different forms or structures (‘polymorphs’) of the same macromolecule, and dictate their usability in a scientific or industrial context. To gain control over an emerging polymorph, one needs a molecular-level understanding of the pathways that lead to the various macroscopic states and of the mechanisms that govern pathway selection. However, it is still not clear how the embryonic seeds of a macromolecular phase are formed, or how these nuclei affect polymorph selection. Here we use time-resolved cryo-transmission electron microscopy to image the nucleation of crystals of the protein glucose isomerase, and to uncover at molecular resolution the nucleation pat...
Source: Nature - Category: Research Authors: Tags: Letter Source Type: research