Study on Purification and Crystallization of Hypothetical Protein AF1514 from Archeoglobus fulgidus

Abstract

Abstract: Archeoglobus fulgidus DSM 4304 genome was transformed and overproduced in Escherichia coli (E. coli BL21)at 12 ℃ and the protein was purified to 95% purity by Ni2+-affinity column and Superdex-75 gel filtration. Crystals ative and methylated proteins were obtained by the hanging-drop vapour-diffusion method at 16 ℃ under three conditions among the wide range of screened conditions (>400), but principally from the solution containing 0.1mol/L sodium acetate pH 5.0, 0.1mol/L sodium chloride, and 8%～14% (W/V) 2-methyl-2,4-dipentaneol (MPD). The crystal is tetragonal in shape and diffraction data to 2.09A0 are detected by X-ray detector.

Key words: , Archeoglobus fulgidus； protein AF1514； crystallization； purification；

PA Zi-Lai-Ti-·Bai-He-Ti, LIU Zhi-Jie, A Bu-Du-La-·A-Ba-Si. Study on Purification and Crystallization of Hypothetical Protein AF1514 from Archeoglobus fulgidus[J]. FOOD SCIENCE, 2008, 29(9): 338-343.

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Study on Purification and Crystallization of Hypothetical Protein AF1514 from Archeoglobus fulgidus

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