S. Wakatsuki et al., BLUE FORM OF BACTERIORHODOPSIN AND ITS ORDER-DISORDER TRANSITION DURING DEHYDRATION, Biochimica et biophysica acta. Bioenergetics, 1185(2), 1994, pp. 160-166
Freshly-prepared blue membranes from Halobacterium halobium, previousl
y reported to be disordered, are shown to have a distinct crystal latt
ice structure, slightly different from the native form. The lattice of
the blue form is disrupted irreversibly when dehydrated. The disorder
process was observed using time-resolved small-angle X-ray diffractio
n and analyzed by radial autocorrelation functions. The diffraction pe
aks of the in-plane lattice first sharpen and increase due to improved
membrane orientation, then the trimer lattice becomes disordered and
the unit cell dimension decreases by 1.8 Angstrom. In contrast, dehydr
ation of purple membranes does not disorder the lattice, and the unit
cell dimension shrinks by only 1.0 Angstrom. Comparisons of radial aut
ocorrelation functions for the blue membrane during drying show drasti
c loss of inter-trimer, long-range correlation while the intra-trimer,
short-range correlations remain more or less unchanged. This suggests
that the deionized protein trimers can maintain their overall structu
re during the dehydration, even though the lattice dimension decreases
appreciably and the two-dimensional crystallinity is disrupted.