The Cloning, Expression, Purification And Preliminary Crystal Growth Study Of Sf2523and PeCBL1

After the human genome project (HGP) was completed,post-genome era has come.Protein Science has become the most active subject frontier in life science and biotechnology.Protein structure data is a key foundation for protein research,especially for the interpretation of protein function.Structural biology came into being as an emerging discipline.This paper focuses on protein expression.purification and crystallization.It selected the antioxidant protein Sf2523in Shigella flexneri2a and the signal protein PeCBL1in Populus euphratica as the object of study.It has successfully constructed the prokaryotic expression system,expressed the target protein Solubly,obtained a high purity of the protein by affinity chromatography,molecular exclusion chromatography,ion exchange chromatography and other methods,and maked a preliminary crystallization screening.The Sf2523protein has got a better three-dimensional monocrystalline.The PeCBLl protein has only observed a microcrystalline,which was still needed a further optimization experiment.During the crystallization optimization of Sf2523protein,it has took the smaller neglected His-tag label into account after conventional optimization methods can not get the desired results.By digesting the lable,the crystallization behavior of Sf2523protein has been greatly improved.