cryoelektronimikroskopiaa

Cryoelektronimikroskopiaa, often abbreviated as cryo-EM, is a powerful microscopy technique used to determine the three-dimensional structure of biological macromolecules. It involves rapidly freezing a sample in a thin layer of vitreous ice, preserving its native state. This frozen sample is then imaged using a transmission electron microscope. Multiple images of the same molecule, taken from different angles, are computationally combined to reconstruct a high-resolution 3D model. The development of direct electron detectors and advanced image processing algorithms has revolutionized cryo-EM, enabling researchers to resolve structures at near-atomic detail. This technique is particularly valuable for studying large and complex molecular assemblies, such as viruses, ribosomes, and membrane proteins, which are often difficult or impossible to crystallize for X-ray crystallography. Cryo-EM has played a crucial role in advancing our understanding of fundamental biological processes and has accelerated drug discovery efforts by providing detailed structural information of therapeutic targets. Its ability to image samples in a near-native hydrated state offers significant advantages over other structural biology methods.