Obtaining well diffracting crystals and solving protein structure can be tedious work and successful process may include various crystallization techniques and tricks. Here we present one didactic story of crystallization α-L-Rhamnosyl-β-D-glucosidase (Rutionsidase) from Aspergilus niger. During the crystallization process, we performed screening using vapour diffusion method, optimization by counter diffusion technique, and final crystals soaking of heavy atoms in micro batch experiments, which allowed structure solution by SIRAS. However, to repeat the crystal growth, we had to deglycosylate the enzyme and perform new screening followed by Matrix Microseed Screening. Moreover, as final reproducible procedure, for growing the protein crystals, we used under oil micro batch experiments. With this optimised method, we were able to grow crystal that diffracted upto 1.27 Å resolution and see structural details that shall be used in the future.