This report concerns structural forces in resting muscle and proposes three additions to the sliding filament model to account for these mechanical properties. The proposal includes: connecting filaments (C-filaments) which connect the ends of each thick filament to the neighboring Z-lines, core filaments which support the myosin of the thick filament and which attach to the C-filaments, and side-struts which bind the thick filaments together along their length and restrict their radial movement. C-filaments would act as the parallel elastic element and transmit the passive tension to the thick filaments. Isolated myofibrils (mechanically-skinned and detergent-treated frog semitendinosus fibers) when stretched progressively showed exponentially-increasing passive tension which did not disappear when filament overlap was exceeded, but continued to rise. SL was monitored with a HeNe laser. Passive tension phasically exceeded 3 X 10(5) N/M2. Electron microscopy (thin-sectioned and freeze-fracture/deep-etch specimens) of non-overlap fibers showed orderly fibril structure with clear separation of A- and I-bands. In the gap between them could be seen filaments, 40-50 A in diameter, connected to the thick filament ends. Unlike actin, these filaments did not become decorated by myosin S-1. Equatorial X-ray measurements showed that stretching relaxed skinned muscles squeezed the thick filaments closer; this radial compression continued beyond filament overlap. Extreme stretch of fibers caused the thick filaments to strain several-fold. Treatment of non-overlap fibers with a high ionic strength pyrophosphate myosin solvent caused a large drop in passive tension and stiffness, but no change in SL was detected nor was myofibril continuity detectably affected. Non-overlap fibrils, when treated with elastase, released A-segments which retain three-dimensional coherency . Deep-etch EM's of non-overlap fibers disclosed abundant structures (about 75 A) wide attaching adjacent thick filaments.