T cells play a critical role in the adaptive immune response. They perform their function by recognizing infected cells presenting peptides on a specialized complex known as the MHC. The recognition process involves binding of the peptideloaded MHC to the T cell receptor (TCR), a surface molecule comprised of an alpha and a beta chain. A large body of evidence suggests that T cells can respond to previously unseen pathogens, a phenomenon known as cross-reactivity. Crossreactivity has important medical implications, as cross-reactive responses can be either protective or lead to disease. A possible mechanism that has been proposed to explain cross-reactivity is the differential usage of the alpha and beta chains, whereas one peptide can be recognized predominantly by the alpha chain and a different peptide by the beta chain. In this study we carry out a systematic analysis of a non-redundant set of 67 crystal structures, measuring TCR alpha/beta usage and its relationship with structural features of the interaction. Our results show a wide range of TCR alpha/beta usage in different complexes. Further, we find that alpha/beta usage significantly correlates with one of the docking angles between the TCR and the MHC.