AbstractThe fine structural appearance of Z‐disk lattices in vertebrate skeletal “fast” muscle varies depending upon whether osmium or glutaraldehyde has been employed as the primary fixative. Prior investigators have attributed the differences to change in the extent of actin filament overlap within the Z‐disk and/or to rearrangement of Z‐disk filaments.Adult frog and young newt “fast” muscle has been studied under various degrees of stretch, with several different aldehyde and osmium fixation procedures, and after plastic section digestion techniques utilizing Pronase or pepsin. Serial cross sections of Z‐disks were correlated with oriented cross and longitudinal sections. Fixation with collidine‐buffered osmium and veronal acetate‐buffered glutaraldehyde seems to provide the greatest and most distinctly contrasting differences. A consistently arranged phase, the filamentous lattice, can be discerned after either fixation. However, a second phase, termed “Z‐disk matrix,” appears variable, perhaps due to extraction during primary osmium fixation procedures. Glutaraldehyde‐fixed frog muscle Z‐disks display a copious matrix, one which is seldom totally depleted by osmium fixation. In young newt muscle Z‐disks, little matrix is present after glutaraldehyde fixation and none of it remains after primary osmium. In Z‐disks fixed by either method, matrix that is retained appears to be deposited in lattice‐like patterns. It is suggested that these matrix patterns, or their loss, are the basis for the varying images of Z‐disks observed under diferent fixation conditions and that the filamentous lattice is relatively stable. The Z‐disk is more rapidly obliterated by Pronase or pepsin digestion than is any other muscle component, including actin (which appears notably unreactive). The rapid digestion effect is limited to the region postulated to include the matrix phase. Models for the structural interrelationship of filamentous and matrix phases are discussed and compared to prior Z‐disk models.