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Protein crystallization has been studied for over 150 years but is still not well
understood. Protein crystals are extremely difficult to grow since protein crystallization is
sensitive to many parameters. In this thesis I investigate if the chirality of a precipitant, 2-
methyl-2,4-pentanediol (MPD), influences the crystal growth of the protein lysozyme. It
appears that R-MPD has a single conformation within the crystal, while S-MPD may take on
a few different conformations. Although there appears to be a chiral difference within the
structure, this does not seem to dramatically affect the kinetics of crystal growth as both
crystal structures form in the same period of time.