The method of electron crystallography is considered as an instrument of structural biology, an alternative to x-ray crystallography. The new CRYOARM 300 transmission microscope was tested to collect electron diffraction data for the analysis of the three-dimensional structure of protein macromolecules. The results of analysis of thin three-dimensional crystals of catalase and membrane protein complex ExbBD are presented. By filtering electrons by energy, the quality of the data has improved markedly. The features of the interaction of electrons with a biological sample embedded in thin vitreous ice cooled to low temperatures are described. The advantages of using electrons of higher energies and filtering electrons with energy losses in electronic three-dimensional crystallography are shown.