The sandwich method for protein crystallization and its effect on crystal growth

Abstract

A device has been invented for protein crystallization by sandwiching the liquid droplet between two surfaces, in which both hydrophilic and hydrophobic surfaces can be used as crystallization substrates. Comparing with the traditional hanging drop method, it can also reduce the evaporation rate of the liquid droplet and provide a stable environment for the crystal growth. In this work, crystal growth experiments for several proteins, especially on the hydrophilic substrate of mica, have shown the positive effect on crystal growth for improving crystallization conditions and the quality of crystals. The features of this new sandwich method and its mechanism have also been discussed.

Structural insight into the cooperation of chloroplast chaperonin subunits

“…The crystallization of functional hetero-oligomers of CPN60 did not succeed, whereas the crystallization of CPN60β1 homo-oligomers was achieved by the sandwich method [ 42 ]. The crystals belong to space group P21, with 14 subunits per asymmetric unit.…”

Three-dimensional Raman spectroscopic imaging of protein crystals deposited on a nanodroplet

“…Reports indicate that the mechanism of protein crystallization is affected by the depth of the microchannel 15 and the nature of the solid surface. [16][17][18][19] In the previous report, we demonstrated that the volume and shape of the nanodroplet influence the protein crystallization behaviour, i.e. the number of crystals and the induction time.…”