Two human renal biopsies containing glomerular amyloid deposits organized into spicular formations (spicular amyloid) were studied by scanning electron microscopy following removal of the cellular components (acellular SEM). Following SEM studies, portions of the same acellular tissue were embedded in paraffin and plastic for light microscopy and transmission electron microscopy, respectively. Spicular deposits by acellular SEM appear as tapering conical formations interconnected by a delicate branching network of fibrils, which imparts a higher degree of organization than previously appreciated by two-dimensional LM and TEM. Silver stains of paraffin- and plastic-embedded acellular tissue showed persistence of argyrophilia in spicular deposits, while acellular TEM showed that the spicules appeared comprised "purely" of amyloid fibrils without visible contaminating material. We conclude that the argyrophilia of spicular amyloid is an inherent feature of the parallel organization of fibrils rather than a result of incorporation of glomerular basement membrane or cell components and that spicular amyloid deposits have a higher degree of organization than is apparent by two-dimensional studies.