Correlation averaging of a badly distorted lattice: the surface protein of Pyrodictium occultum.

Abstract

The surface protein of the archaebacterium Pyrodictium occultum forms two-dimensional periodic arrays of extremely poor order. Two variants of correlation averaging have been applied in order to retrieve the unit cell structure from electron micrographs of negatively stained samples: straightforward correlation averaging correcting for lateral displacements only and a more elaborate approach, including a partial compensation for rotational disorder. Surprisingly, both routes yield virtually identical structures. Inclusion of molecular motifs from highly disordered domains, which are rejected in the "straightforward" approach, appears not to improve resolution, possibly because the high local strain tends to distort the individual molecules.