The correlation averaging of a regularly arranged bacterial cell envelope protein

Abstract

An adaptation of the 'correlation averaging' method is described which allows reliable and almost fully automatic image averaging in the case of near-periodic structures notwithstanding the presence of substantial crystal imperfections; methods for assessing resolution and symmetry without reliance on crystallinity are also discussed. Electron micrographs of negatively stained and rotary shadowed preparations of the HPI-layer protein from the cell envelope of Micrococcus radiodurans have been averaged using the method, and the projected structure is described to a resolution of about 1.9 nm.