厦门大学学报（自然科学版）2017，Vol.56Issue(1)：64-71,8.DOI:10.6043/j.issn.0438-0479.201604036
人源Pelota C端结构域的纯化、结晶及晶体结构分析
Purification,Crystallization and Crystallographic Analysis of the Pelota C-terminal Domain from Human
摘要
Abstract
Pelota,an evolutionarily conservative RNA binding protein,is distributed in almost all tissues and involved in a variety of cell biological regulation as a multifunctional protein.In order to determine the crystal structure of the human Pelota C domain (C-terminal domain,CTD),we chose Escherichia coli to express the protien and purified the protien by affinity chromatography,gel fil-tration chromatography.Finally,the protein is over 97% in purity.Dynamic light scattering experiments showed that the purified pro-tein had high homogeneity.After screening the 1 852 crystallization conditions,the optimized crystal of the human Pelota C domain can be diffracted to 0.26 nm resolution.The space group of the crystal is P65 22,and the unit cell constant is a=7.882 nm,b=7.882 nm,c=19.746 nm.We determine the crystal structure of human Pelota CTD in this study,which lays a foundation for further study on the function of Pelota protein and its interaction with the downstream proteins.关键词
Pelota C端结构域/人源/表达/纯化/结晶Key words
Pelota C-terminal domain/human/expression/purification/crystallization分类
生物科学引用本文复制引用
张兰君,靳林丹,任海霞,林天伟..人源Pelota C端结构域的纯化、结晶及晶体结构分析[J].厦门大学学报（自然科学版）,2017,56(1):64-71,8.基金项目
高等学校学科创新引智计划(“111”计划)(B06016) （“111”计划）
