Crystallization & Structure Determination
Dr. Orly Dym, Head
Meyer building #109
The crystallization facility at the ISPC utilizes several parallel approaches to determine and analyze the 3D structures of proteins and protein complexes. This challenge requires the seamless integration of expertise with the state-of the art robotics with which the facility is equipped. The aim of protein crystallization is to produce well-ordered protein mono-crystals large enough to diffract X-ray beams. Finding the right crystallization conditions is a tedious trial-and-error process that involves screening precipitants and examining different crystallization methods, utilizing various robots, and working at two temperatures, 4ºC and 19ºC. Once a suitable crystal has been obtained, X-ray data are collected either on an in-house source or at a synchrotron facility, and are then used to solve the 3D structure of the protein. To take full advantage of a structure so obtained, we perform detailed comparative sequence-based-structure analysis of the protein itself and of related proteins so as to gain insight into its mode of action, specificity and biological relevance.