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The high resolution structure of protein molecules and protein-protein complexes is important to investigate their functions. Today, large 3D or 2D crystals are required to obtain protein structures by X-ray crystallography or conventional Electron Microscopy, respectively. However, production of such crystals of good quality is a solely empirical procedure, which relies on screening numerous crystallization conditions. At the same time, multilayered protein crystals are often a by-product of attempts to grow 3D or 2D crystals and could be obtained more easily. So far, multilayered protein crystals have not been used in electron microscopy for structure determination, as the interpretation of an electron diffraction pattern is rather complicated. In this thesis we present the first protein structure bovine liver catalase at 4 Å resolution solved using electron diffraction data from multilayered crystals. 55 diffraction patterns (17 tilt series) were recorded and used for the reconstruction. The tilt geometry of each individual diffraction pattern was determined by a least-squares algorithm or Laue zone analysis to perform spot indexing. The phase problem was solved by molecular replacement. The influence of the missing data cone on the self-rotation function and interpretation of reconstructed map is discussed.