Single particle cryo-electron microscopy (cryo-EM) is a structural biology method used for solving high resolution structures of proteins and their complexes. Due to recent advances in hardware and software it becomes more and more popular. In comparison to crystallography, where crystal growth constitutes a serious bottleneck of structure solution process, in cryo-EM protein particles are frozen in liquid like state of vitreous ice and imaged under electron microscope. Following that, particles are selected and classified to generate 2d classes. Next these 2d classes are used to reconstitute density maps of the studied particles which then can be further used for model building.

In Max Planck Research Group we are utilising cryo-EM to study 850 kDa eukaryotic Elongator complex responsible for initial modification of wobble uridine at C5 position of selected tRNAs. In addition to that we are also interested in how Elongator is regulated by Kti11, Kti12, Kti13 and Kti14 proteins. Structural biology core facility in Malopolska Center of Biotechnology of Jagiellonian University (JU) is equipped with JEOL HDT-400 glow discharger, FEI Vitrobot Mark IV and Molecular Dimensions grid box storage system, everything that is needed to prepare and store cryo-EM samples. Cryo grids are screened on JEOL JEM2100 HT CRYO LaB6 electron microscope installed in the Department of Cell Biology and Imaging in the Institute of Zoology and Biomedical Research JU.