Collagen fibrils with a symmetric banding pattern, an as yet overlooked component of the extracellular matrix, were found in the reticular layer of the basement membrane of human sebaceous glands. In longitudinal sections this newly described banding pattern is D-periodic (D = 67 nm) resembling the period length of native type collagen fibrils. In cross sections the symmetrically banded fibrils are irregularly outlined. The period length and the symmetric banding pattern led to the assumption that collagen molecules are staggered by the distance D, similar to native type collagen fibrils, but are arranged antiparallel. This hypothesis was tested by antiparallel superposing transparent photocopies of native type fibrils. In addition, schematic drawings of the cross striation pattern of native type fibrils were superposed in reverse directions by means of computerized image-manipulation. A model of molecular alignment was evolved from these experiments, which is characterized by two features: 1) pairs of antiparallel collagen molecules are D-staggered and 2) the two molecules of a pair are slightly shifted from precise register. The proposed model is the only one correlating with the data obtained from direct measurements on symmetrically cross striated fibrils. The fibrils described in the present study represent a supramolecular aggregate of collagen previously not observed in vivo.