Effects of the silanized mica surface on protein crystallization.
A freshly cleaved mica surface silanized by 3-aminopropyl triethoxysilane is flat over a large area, displays a controlled degree of hydrophobicity and contains positive charges. In this paper, mica sheets silanized by this method have been used as crystallization surfaces for lysozyme, trichosanthin and three other proteins of unknown structure. Crystallization experiments have been carried out by the hanging-drop vapour-diffusion technique and the results indicate that the silanized mica surface can ameliorate the protein crystallization process considerably compared with a silanized glass cover slip control. For lysozyme on the silanized mica surface, the induction time required for crystal growth decreases markedly. For trichosanthin, the crystal size is obviously larger and the number of crystals grown is much lower. For the three proteins of unknown structure, the diffraction ability of the crystals is improved considerably.