  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.
