Abstract
The detailed distribution of stain grains in contact with the stain-excluding portions of a protein molecule is random: inspection of a single image of a macromolecule reveals little below the resolution level of gross morphology (Fig 1). However, new insights can be gained by analyzing a large set of molecule images resulting from the same experiment.Firstly, the noise reduction due to averaging allows higher-resolution detail to be retrieved. Secondly, the analysis of such a set reveals new information that is qualitatively different from information contained in a single molecule image: the patterns of variation in local stain distribution. The stain variation at any point, and the way in which stain variations at different points of the structure are correlated, reflect certain constraints that have to do with the local binding characteristics of the molecule (e.g. accessibility of charged sites) and with its detailed topography. In the past, few observations were made relating to these phenomena because they are very difficult to quantify.
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