The correlation averaging of a regularly arranged bacterial cell envelope protein

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Abstract
SUMMARY: 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.