Random Microseed Matrix-Screening (rMMS), where seed crystals are added automatically to random crystallization screens, is a significant recent breakthrough in protein crystallization [1]. During the ten years since the method was published, understanding of the theoretical advantages of the method has increased [2 - 4], and several important practical variations on the basic method have emerged. Important variations include combining seeds from several hits [5], the best methods of selecting hits to optimize [2], and cross-seeding targets with crystals of homologous proteins [6]. We also present an approach that allows the method to be applied to the crystallization of membrane proteins in LCP [7], and a novel approach to preparing samples for cryoEM.