The present findings establish that bone from a patient with BS2, caused by compound heterozygous PLOD2 mutations, has telopeptide lysine underhydroxylation and a cross‐linking abnormality that phenocopies that of BS1 bone caused by functionally null FKBP10 mutations.(20) This supports the evidence that lysyl hydroxylase‐2b encoded by PLOD2 forms a complex with FKBP65(16, 18) encoded by FKBP10, which is required for normal collagen cross‐linking in bone and certain other skeletal tissues. The gene discussed is PLOD2; the disease is Biemond syndrome type 2.