Three-dimensional structures have recently been determined by electron crystallography at a resolution high enough to determine atomic arrangements in both protein and mineral specimens. The different nature of these two types of specimens produces some very significant differences in the way data is obtained and processed, although the principles are the same. The sensitivity of proteins to damage by the electron beam limits the signal-to-noise ratio in the image and the resolution to which data can be extracted from the image. A number of constraints, such as the amino acid sequence and the connectivity of atoms within amino acids, can be used in interpreting the limited image data. In materials samples, the relative insensitivity to damage allows obtaining resolution limited only by the microscope. In many samples, dynamical scattering and other non-linear effects limit the information in the image, but this limit can be circumvented by working in very thin areas of the specimen.
Downing, Kenneth H.
"Three-Dimensional Crystallographic Reconstruction for Atomic Resolution,"
Scanning Microscopy: Vol. 1992
, Article 4.
Available at: https://digitalcommons.usu.edu/microscopy/vol1992/iss6/4