The human genome has been sequenced for decade, but solving how proteins fold and assemble into complexes remains a challenge. More than half of all proteins-including 95% of integral menbrane proteins-do not crystallize and thus their structures cannot be determined by crystallography. We address this problem by creating an instrument that can determine atomic-resolution structures (better than 2A) of individual biological macromolecules without requiring crystallization. Taking advantage of the cooling effect and the superfluidity of helium droplets, we can effectively induced orientation/alignment using a polarized laser. The ability to manipulate the alignment of the diffracting molecule using an elliptically polarized laser field enables structure refinement in three-dimensions. We have recently applied this orientation method for coherent electron diffraction of phthalocyanine gallium chloride. Progress reports of electron diffraction from the dopant molecule and in an alignment laser field will be presented.