Two-dimensional (2-D) crystallization experiments at the water-air interface with recombinant apoferritin (horse liver) are described using a recently developed protein spreading technique, which is based on density and surface tension differences of the subphase and the injected protein solution. The preparation protocol was modified to investigate the influence of additives such as glutaraldehyde and CdSO 4 on the crystallization process. The crystalline arrays were examined by electron crystallographic techniques. It turned out that addition of the cross-linker glutaraldehyde to the subphase buffer was crucial for maintaining the integrity of a fragile 2-D crystal of the square lattice type, which was not observed previously during transfer onto electron microscopy grids.
The formation of two-dimensional (2-D) crystals of biological macromolecules is of interest for nanotechnological applications. Protein 2-D crystals may be used as molecular sieves and/or support devices as components of biosensors etc. [1]. Functionally specialized 2-D crystals, containing transport or catalytic proteins, provide a certain function in a highly efficient and vectorial manner. Future developments may allow the design of more complex structures such as multilayers made from different proteins or arrays of functionally linked oligo- or multimeric complexes consisting of multiple protein species [2]. Regular 2-D arrays, either truely crystalline or densely packed molecules, are one of the basic structures taht might be used to construct more sophisticated protein-based devices. 2-D crystals have some interesting features:
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