Biological molecules often crystallize either as tubes, having helical symmetry, or as two-dimensional sheets. Both sorts of crystal are potentially suitable for structure determination to atomic resolution by electron crystallography, but their lattice distortions must first be corrected. We have developed a procedure for tubular crystals, based on independent alignment of very short segments against a reference structure, that allows accurate determination and correction of distortions in all three dimensions. Application of this procedure to images used previously to determine the 9 A structure of the acetylcholine receptor showed that about half of the signal loss caused by the distortions arises from effects correctable in the image plane (bending, changes in scale) and half from effects requiring out-of-plane correction (variations in tilt and in twist around the tube axis). By dividing the tubes into short segments (of lengths about equal to their diameter) it became possible to recover almost all of this loss without reducing appreciably the accuracy in the segmental alignments. The signal retention improved by only 10% at low resolution (20 A), but by progressively greater amounts at higher resolutions, up to approximately 40% at 9 A. As a result the finer structural details were more clearly resolved. With images of better electron-optical quality, much greater gains in signal retention should be obtained.