Abstract
The crystal growth of biological macromolecules is a very complicated process involving numerous parameters, such as pressure, pH, micro-gravity, photochemical and mechanical induction of nucleation. The utilization of Langmuir–Blodgett (LB) thin film as a template plays an important role in order to produce well-diffracting, stable and radiation-resistant protein crystals. LB nanotemplate crystallization method is a modification of the classical hanging drop vapor diffusion method. We tested four standard proteins, changing different parameters such as protein and salt concentration, number of LB layers etc., in order to verify the real role of LB template. Our results suggest that LB template essentially acts in two way on crystallization: in nucleation and in crystal growth. The possible explanation of these effects is also discussed.
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