DIRECT OBSERVATION OF DEFECT STRUCTURE IN PROTEIN CRYSTALS BY ATOMIC FORCE AND TRANSMISSION ELECTRON-MICROSCOPY

We have examined the structure of S-layers isolated from Sulfolobus acidocaldarius using atomic force microscopy and transmission electron microscopy (TEM). From the AFM images, we were able to directly observe individual dimers of the crystal, defects in the crystal structure, and twin boundaries. We have identified two types of boundaries, one defined by a mirror plane and the other by a glide plane. This work shows that twin boundaries are highly structured regions that are directly related to the organization of units within each crystal domain. Projection maps from TEM images have shown that there are significant differences in the final average maps, depending on which side of the sample is adsorbed to the carbon support film. Comparison of AFM images to TEM projection maps has allowed us to relate high magnification views obtained by AFM to the relatively high resolution information obtained by electron microscopy and image processing.