拟南芥AtCBL9蛋白的原核表达纯化及其晶体生长研究  

Expression,Purification and Crystal Growth of AtCBL9 of Arabidopsis thaliana

作　　者：赵子华[1] 赵田欣[1] 丁志强[1] 尚桂军[1,2] 聂荣鑫[2] 李娜[2] 

机构地区：[1]北京林业大学理学院,北京100083 [2]中国科学院生物物理研究所,北京100101

出　　处：《西北植物学报》2011年第6期1115-1119,共5页Acta Botanica Boreali-Occidentalia Sinica

基　　金：国家"973"计划(07971002)

摘　　要：将拟南芥AtCBL9基因构建入原核表达载体pET-22b(+),在大肠杆菌中得到大量表达,用亲和层析和分子筛排阻层析2种方法对表达蛋白进行纯化。SDS-PAGE和动态光散射分析结果显示,AtCBL9蛋白在体外主要以单体和二体形式存在,单体和二体为同一蛋白,并具有较高的纯度。从单体蛋白中筛选出了微晶,为AtCBL9晶体生长优化及其最终结果解析和功能阐明奠定了基础。AtCBL9 was constructed into the expression vector pET-22b（＋）,overexpressed in the E.coli,and then protein has been purified through two steps chromatography.SDS-PAGE and DLS analysis shows that AtCBL9 protein mainly exists as monomer and dimmer in vitro,the monomer and dimmer are the same protein,and AtCBL9 protein has high degree of purity.Finally microcrystal was selected from monomer protein.These works provide the first step for its structure determination,or rather,its function illumination from molecular level.

关 键 词：AtCBL9蛋白 蛋白表达 蛋白纯化 晶体生长 

分 类 号：Q816[生物学—生物工程]