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Ultrastructural studies of the localization of serum amyloid P component (SAP) in amyloid ®brils have given divergent results. We here report for the ®rst time that electron microscopy of SAP coincubated with Ab 1±42 peptides or with mature Ab 1±42 ®brils, revealed SAP molecules coating the surface of the mature ®brils and that proto®brils of Ab 1±42 did not bind SAP. Also when incubated with extracted amyloid light chain (AL)-®brils the SAP molecules aligned on the ®bril surface. Heparan sulfate proteoglycan bound to the surface of the Ab ®brils with a spacing of about 50 nm. We conclude that SAP does not bind to proto®brils but to the surface of mature Ab ®brils and that it may stabilize and protect the ®brils.

Clone detection results are often voluminous and difficult to present. Most clone presentations focus on the quantitative clone results but do not relate them to the structure of the analyzed system. This makes it difficult to interpret the results and draw conclusions. We suggest using edge bundle views to interrelate the system's structure with the clone detection results. Using this technique, it is easier to interpret the clone results and direct further analysis effort.