hIntL-1 is a disulfide-linked trimer as shown by non-reducing SDS-PAGE and X-ray crystallography. Despite lacking the intermolecular disulfide bonds, XEEL-CRD is trimeric in solution. The N-terminal peptide of the full length XEEL is responsible for dimerizing the trimeric XEEL-CRD into a disulfide-linked hexameric full-length XEEL. Therefore, the N-termini of intelectins are often responsible for forming disulfide-linked oligomer. In intelectin homologs where the N-terminal cysteines are absent, the CRD itself may still capable of forming non-covalent oligomer in solution.