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A three-dimensional model of the protein arrangement in the Escherichia coli 30S ribosome was constructed by using computerized multidimensional scaling of immunoelectron microscope data. This enabled data comparison between the new electron microscope technique and other methods such as crosslinking, chemical protection, affinity labeling, energy transfer, and assembly interactions. The immunoelectron microscopy data are reasonably consistent with those from other sources. Reasons for some inconsistent data are discussed and our calculation of the dimensions of the proteins, both globular and elongated, are summarized.

proceedings of the national academy of sciences of the united states of america

Use of computerized multidimensional scaling to compare immunoelectron microscopy data with protein near-neighbor information: application to the 30S ribosome from Escherichia coli.