Heterogeneous nucleation and single crystal growth of hen egg-white lysozyme on glass plates
1991
Fukuba, Y. (Hiroshima Univ., Fukuyama (Japan). Faculty of Applied Biological Science) | Sato, K.
X-ray structural analyses for molecular structures of proteins have been most convincing and informative. In the course of the X-ray analysis, growth of protein crystals of high quality is the most difficult process and the mechanisms of protein crystal growth have been less known in comparison to small molecule crystals. Hence, fundamental studies are highly needed to fully understand the protein crystallization processes. In this study, we tried to crystallize large-size single crystals on glass plates which were inserted in a growth solution, using hen egg-white lysozyme as model of protein. Heterogeneous nucleation process played an important role in this crystallization technique. The following results were obtained: 1) Orthorhombic form single crystals were grown under the present growth conditions, 2) heterogeneous nucleation was promoted at higher concentration of precipitant, 3) crystals were grown on the glass plates, 4) it was easier to grow large crystals by inclining the glass plates in the solution, 5) single crystals having the maximum dimensions of 10 mm in length and 3 mm in width and 2 mm thickness could be crystallized. Using the large-size single crystals obtained with this method, one can characterize the protein crystals such as crystal perfection, surface microtopography, and crystal growth process etc
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