The recent publication of a 3-D image of isolated Z-disks from Apis mellifera, flight muscle[Rusu et al., J. Muscle Res Cell Motil (2017)], the first of its kind utilizing isolated Z-disks, confirmed many details of the previously 3-D image obtained from plastic sections[Cheng and Deatherage, J. Cell Biol. (1989)]. However, they used relatively harsh treatment of high KCl/KI to isolate Z-disks. Here we combine 1.4M NaCl and 10mM pyrophosphate applied to Lethocerus indicus flight muscle to remove the thick filaments and 4.5min exposure to calcium insensitive gelsolin to remove the thin filaments from the remaining of the I-Z-I-brushes. We are improving the resolution by adding more tilt-series to our previous analysis. By comparing the Fourier transforms and subvolume averages, we conclude that Z-disks from honey-bee and Lethocerus indicus are similar but not identical. The large solvent channel that characterizes the honey-bee Z-disk is less prominent in Lethocerus, which is reflected in a much weaker to nearly absent 1,0 spot intensity in transforms of Lethocerus Z-disks, whereas the corresponding spots in the honey-bee transform are strong. There is ample evidence that the actin filaments in the overlap zone of both bee and waterbug flight muscle present a helical array of target zones around each thick filament. However, Squire[J. Molec. Biol. 72, (1972)] has pointed out that the P312 symmetry assumed for the honey-bee Z-disk reconstruction from plastic sections when extrapolated into the A-band, implies rings rather than helices of target zones surrounding the thick filament. This discrepancy might be resolved if there are three-fold screw axes instead of three-fold rotation axes at the lattice and trigonal positions of the flight muscle Z-band; corresponding more to space group symmetry P3121.