Aim: To prepare and identify the aggregates of A53T and A30P mutant of α-synucleins (α-Syns) linking to familial Parkinson disease to provide important theoretical bases and targets for the treatment and rehabilitative intervention of Parkinson disease. Methods: The experiment was performed in Research Department of Neurobiology, Beijing Institute of Geriatrics, Xuanwu Hospital, Capital University of Medical Sciences from January to May 2004. The PCR primers containing proper enzymatic sites were designed. The encoding sequences for human A53T and A30P α-Syns were subcloned into the pGEX-4T-1 expression vector of glutathione S-transferase (GST) fusion protein synthesized from pBS-α-Syn (A53T) and pBS-α-Syn (A30P). The reconstructed plasmids pGEX-α-Syn (A53T) and pGEX-α-Syn (A30P) were transformed into E. coil BL21, and the fusion proteins GST-α-Syn (A53T) and GST-α-Syn (A30P) were induced by isopropyl-D-thiogalactopyranoside (IPTG), purified by Glutatione Sepharose 4B column affinity chromatography and digested with thrombin to obtain recombinant A53T and A30P α-Syn proteins. After lyophilized, the proteins were incubated at 37 °C C for 2 hours to make aggregated mutant α-Syns in vitro. The protein aggregates were identified using Western blot analysis and transmission electron microscopy. Results: DNA sequence analysis proved correct reconstruction of A53T and A30P. The purified recombinant A53T and A30P α-Syns were separated on SDS-PAGE as a single band of 18 ku, which was identical to the reported molecular size of this protein. Western blot analysis showed that the mutant proteins and their aggregates could be recognized by an antibody specifically against α-Syn. The size of the aggregated α-Syns was about 108 ku, equal to the size of α-Syn hexamers. The aggregated α-Syns under electron microscope represented short filamentous structures. Conclusion: The above results suggest that the aggregate models of the mutant human α-Syn A53T and A30P have been successfully produced in vitro. The result can provide an important material basis for etiology of Parkinson disease and a new target for recovery of patients with Parkinson disease.