抄録
This experiment was conducted using the microgravity environment in space to prepare single crystals of good crystallinity in which protein molecules are very well ordered. Five kinds of protein samples: hen egg-white lysozyme (2 different crystallization conditions), horse skeletal myoglobin, ω-Amino acid: pyruvate aminotransferase from Pseudomonas sp. F-126, and Rhizopus niveus lipase, were used for crystallization, which was carried out according to the batch method for 7days at 20°C. Among these protein samples, crystals were produced from the four samples and the particularly noteworthy results could be obtained from lysozyme at pH4.5 and ω-amino acid:pyruvate aminotransferase. In this space experiment, crystal growth proceeded at a slower rate than expected, compared with a control experiment on earth. Furthermore, it was proved that space-grown single crystals possessed a good crystallinity although they were not always of an optimal shape and size for X-ray crystallography. Depending on the protein samples and the crystallization conditions, crystal nuclei grew in different shapes of crystals from those of ground-grown ones due to the influence of the gravity field in space.
