The light driven proton pump bacteriorhodopsin (bR) occurs naturally as two-dimensional crystals. A three-dimensional density map of the structure, at near atomic resolution, has been obtained by studying the crystals using electron cryo-microscopy to obtain diffraction patterns and high resolution micrographs (1).New methods have been developed for analysing micrographs from tilted specimens, incorporating the methods previously developed for untilted specimens that enable large areas to be analysed and corrected for distortions. Data from 72 images, from both tilted and untilted specimens, have been analysed to produce the phases of 2700 independent Fourier components of the structure. The amplitudes of these components have been accurately measured from 150 diffraction patterns. Together, these data represent about half of the full three-dimensional transform to 3.5 Å. The distribution of the data which is included in the map is shown in fig. 1. For specimen tilts up to around 20° the data is essentially complete. For higher tilts the data is more sparsely sampled, and is at present about half complete.
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