Protein crystal growth in low gravity

This research involved (1) using the Atomic Force Microscope (AFM) in a study on the growth of lysozyme crystals and (2) refinement of the design of the Thermonucleator which controls the supersaturation required for the nucleation and growth of protein crystals separately. AFM studies of the (110) tetragonal face confirmed that lysozyme crystals grow by step propagation. There appears to be very little step pile up in the growth regimes which we studied. The step height was measured at = 54A which was equal to the (110) interpane spacing. The AFM images showed areas of step retardation and the formation of pits. These defects ranged in size from 0.1 to 0.4 mu. The source of these defects was not determined. The redesign of the Thermonucleator produced an instrument based on thermoelectric technology which is both easier to use and more amenable to use in a mu g environment. The use of thermoelectric technology resulted in a considerable size reduction which will allow for the design of a multi-unit growth apparatus. The performance of the new apparatus was demonstrated to be the same as the original design