Controlling crystallization and its absence: Proteins, colloids and patchy models

TL;DR

This paper reviews how controlling particle crystallization and its suppression is crucial across biological, colloidal, and material systems, emphasizing insights from biological control, computational modeling, and the concept of frustration.

Contribution

It provides a comprehensive overview of mechanisms controlling crystallization and its absence, integrating biological examples, computational insights, and the role of frustration in diverse particle systems.

Findings

Biological systems suppress protein crystallization but can form functional crystalline assemblies.

Computational models reveal the interplay between interparticle interactions and crystallization kinetics.

Frustration between local and global order influences crystallization behavior in atomic and colloidal systems.

Abstract

The ability to control the crystallization behaviour (including its absence) of particles, be they biomolecules such as globular proteins, inorganic colloids, nanoparticles, or metal atoms in an alloy, is of both fundamental and technological importance. Much can be learnt from the exquisite control that biological systems exert over the behaviour of proteins, where protein crystallization and aggregation are generally suppressed, but where in particular instances complex crystalline assemblies can be formed that have a functional purpose. We also explore the insights that can be obtained from computational modelling, focussing on the subtle interplay between the interparticle interactions, the preferred local order and the resulting crystallization kinetics. In particular, we highlight the role played by ``frustration'', where there is an incompatibility between the preferred local order and the global crystalline order, using examples from atomic glass formers and model anisotropic particles.