Protein crystallography enables us to visualize protein structures at the atomic level and enhances our understanding of protein function. X-ray crystallography was first applied for biological macromolecules (i.e. hemoglobin) in the late 1950s and had been awarded Nobel Prize in Chemistry in 1962, which had a great impact on further development of structural biology. In order to determine the structure, a high-quality crystal of the specific protein is required. Obtaining such crystals is a crucial step in protein crystallography and has been fully automated by developing crystallization platforms, which perform high-throughput screening of hundreds of thousands of experimental conditions to facilitate the optimization of crystallization process. To see proteins in atomic resolution and determine their structure, we need to use electromagnetic radiation provided by synchrotron beamlines. This advanced technique is based on X-rays scattering on molecule atoms that provide a diffraction pattern, used to generate an electron density map and eventually solve the protein structure.

In our laboratory, we use X-ray crystallography to study how proteins interact with other molecules (i.e. tRNA) and gain detailed knowledge about macromolecular assemblies and their role in post-transcriptional regulation. Recently, we have obtained the TEAM-TECH Core Facility grant from Foundation for Polish Science to establish a Structural Biology Core Facility, equipped with highly specialized devices for crystallization trials to reassure maximum efficiency and reproducibility in crystallization pipeline.