J Integr Plant Biol. ›› 1998, Vol. 40 ›› Issue (9): -.

• Research Articles •    

Effect of PEG and Salt on Crystallization of Bacterioferritin and Nitrogenase MoFe Protein from Azotobacter vinelandii

HUANG Ju-Fu, WANG Dao-Yong, Wang Zhi-Ping, LUO Ai-Ling, GU Shu-Rong and LI Jia-Ge   

Abstract: MgCl2 was added to the supernatant of the first crystallization of MoFe protein to give a final concentration of 14.6 mmol/L, followed by centrifugation. The treated supematant solution and MoFe protein could be crystallized by using method of siting drop with PEG 6000 and MgC12 as a precipitant and salt, respectively. The larger crystal from the supermatant was observed when the final concentration of PEG and MgCl2 was 4.5% and 15.6 mmol/L, respectively; but small crystal was observed when the concentration was 0 and 23.8 mmol/L, respectively. The larger crystal in brown rectangular prism of MoFe protein was also obtained using the same crystallization method when the final concentration of PEG and MgCI2 was 7.44% and 338.0 mmol/L, respectively. It suggests that the two protein crystals seem to be different, the former being bacterioferritin and the later as nitrogenase MoFe protein.

Key words: Crystallization, Bacterioferritin, Nitrogenase, MoFe protein, Azotobacter vinelandii

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