▪ Abstract Crystallization is necessary to obtain the three-dimensional structure of proteins
and nucleic acids; it often represents the bottleneck in structure determination. Our …

Recent results on the associations between protein molecules in crystal lattices, crystal–
solution surface energy, elastic properties, strength, and spontaneous crystal cracking are …

Surface morphologies of thaumatin, catalase, lysozyme and xylanase crystals were
investigated using in situ atomic force microscopy. For thaumatin, lysozyme and xylanase …

Particular interest in the role of convection in protein crystallization has arisen since some
protein single crystals of improved structural quality have been obtained under reduced …

Recently, much progress has been made in understanding the nucleation and crystallization
of globular proteins, including the formation of compositional and structural crystal defects …

Interferometric microscopy was used to investigate the growth morphology and kinetics of
{110} and {101} faces of tetragonal lysozyme crystals. Solutions were prepared from as …

Hen egg-white lysozyme (HEWL) is widely used as a model protein, although its purity has
not been adequately characterized by modern biochemical techniques. We have identified …

We have experimentally studied the effects of solution flow on the growth kinetics of the
protein lysozyme. To this end, we have expanded our interferometry setup [Vekilov et al., J …

Dislocations in molecular crystals remain terra incognita. Owing to the complexity of
molecular structure, dislocations in molecular crystals can be difficult to understand using …

Surface morphology and growth kinetics of thaumatin crystals in the supersaturation range
σ= 0− 1.65 were investigated using in situ atomic force microscopy (AFM). At σ< 0.7 growth …