Wr. Schief et al., Two-dimensional crystallization of streptavidin: in pursuit of the molecular origins of structure, morphology, and thermodynamics, BIOMOL ENG, 16(1-4), 1999, pp. 29-38
The streptavidin two-dimensional (2D) crystallization model has served as a
paradigm for molecular self-assembly at interfaces. We have developed quan
titative Brewster angle microscopy for the in situ measurement of spatially
resolved relative protein surface densities. This allows investigation of
both the thermodynamics and morphologies of 2D crystal growth. For crystal
structure analysis, we employ TEM on grown crystals transferred to solid su
bstrates. Comparison of results between commercially available streptavidin
, recombinant streptavidin, and site-directed streptavidin mutants has prov
ided insight into the protein-protein and protein-lipid interactions that u
nderlie 2D crystallization. (C) 1999 Published by Elsevier Science B.V. All
rights reserved.