An approach that enables up to a two order of magnitude reduction in the amount of protein required and a tenfold reduction in the amount of time required for vapor-diffusion protein crystallization is reported. A prototype high-throughput automated system was used for the production of diffractionquality crystals for a variety of proteins from a screen of 480 conditions using drop volumes as small as 20 nL. This approach results in a signi®cant reduction in the time and cost of protein structure determination, and allows for larger and more ef®cient screens of crystallization parameter space. The ability to produce diffraction-quality crystals rapidly with minimal quantities of protein enables high-throughput efforts in structural genomics and structure-based drug discovery.

ZnO-doped lithium niobate crystals with a doped concentration of up to 8.3mol% were grown by the Czochralski technique. The effects of incorporating Zn2+ ions into LiNbO3 crystals were studied by powder x-ray diffraction and taking polarization hysteresis loop measurements. When the Li-site vacancy model is adopted, the coercive fields obtained from the polarization reversal measurement depend strongly on the number of NbLi4−+4VLi−. However, the coercive field of Zn-doped ions into LiNbO3 is insensitive to the ZnLi2++VLi−. Experimental results indicate that four distinct substitutions of Zn−2 ions incorporated into ions into LiNbO3 crystals for doping concentrations from 0to8.3mol%. The extent of Zn substitution is quantitatively determined for doping of below 7.5mol%.