X-ray diffraction of rat tail tendon shows that type I collagen fibrils contain regions of three-dimensional crystalline arrays; where molecular packing is speculated to be by a staggered sheet or microfibril arrangement. The X-ray diffraction pattern also contains a significant amount of diffuse scatter indicative of static and thermal disorder in fibrils. Removal of the diffuse scatter from the equatorial region of X-ray diffraction patterns obtained using synchrotron radiation allowed the Bragg intensities to be viewed on a flat background. Indexing of Bragg peak intensity on the 10, -10, 0 -1, 01, -11 and 1-1 row-lines of the triclinic unit cell have been used here to test possible sheet and microfibril packing arrangements. The relative translation of molecular segments in the gap and overlap regions as well as the telopeptide orientation have been investigated. A global search through combinations of molecular packing and molecular translation revealed that the sheet-type conformations cannot account for the observed low-angle off-meridional Bragg peak intensity distribution. A superior fit is obtained with D-staggered left-handed microfibril structures. The orientation of the telopeptides may indicate that there are interconnections between microfibrils that may explain the difficulty in isolating individual microfibrillar structures.