Surface Reconstruction is the technical
term for the difference between the packing arrangement of the surfaces
of crystals from that in the crystal interior. This is a well known
phenomenon in inorganic crystals. It is believed to occur because
the surface molecules have incomplete bonds and because they are in contact
with the solvent, unlike molecules in the crystal interior. It was
not known if this phenomena would occur in protein crystals, as in these
crystals the molecules in the interior are also in contact with the solvent
phase. While trying to determine the
molecular packing arrangements on tetragonal lysozyme crystal faces with
high resolution AFM, we observed the surface reconstruction phenomenon
for the first time on a protein crystal.
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Figure 1:
Comparison between an experimental AFM image and a theoretical one for the (110) face of tetragonal lysozyme crystals. The theoretical image was constructed for a packing arrangement with complete 43 helices. This packing corresponds to that of the crystal interior obtained from X-ray crystallography. This theoretical image is shown here embedded in the experimental AFM image (see also the section on surface packing). The correlation between the two images is 62%. The whole image has been slightly tilted to show 3D features. |
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Figure 2:
Same image as figure 1, but the theoretical image was constructed by modifying the packing slightly. The molecules were moved closer to the 43 axis by 7Å from the crystallographic arrangement of the interior. The correlation between the new theoretical image and the experimental one is now 93%. |
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