The hemocyanins of molluscs are aggregates of a cylindrical decameric subparticle that assembles into di-, tri-, tetra-, penta-, and larger multi-decameric particles with masses that are multiples of the 4.4 Md decamer. Electron micrographs of these hemocyanins typically show the particles with two profiles: circular representing the cylinder viewed from the end and rectangular representing the side-view of the hollow cylinder.The model proposed by Mellema and Klug from image analysis of a didecameric hemocyanin with the two decamers facing one another with collar (closed) ends outward fits the appearance of side-views of the negatively-stained cylinders. These authors also suggested that there might be caps at the ends. In one of a series of transmission electron microscopic studies of molluscan hemocyanins, Siezen and Van Bruggen supported the Mellema-Klug model, but stated that they had never observed a cap component. With STEM we have tested the end cap hypothesis by direct mass measurements across the end-views of unstained particles.
Mass measurements of neutron-rich nuclei near the N=20 and 28 shell closures
