His-tag impact on structure

被引:184
作者
Carson, Mike [1 ]
Johnson, David H. [1 ]
McDonald, Heather [1 ]
Brouillette, Christie [1 ]
DeLucas, Lawrence J. [1 ]
机构
[1] Univ Alabama, Ctr Biophys Sci & Engn, Birmingham, AL 35294 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2007年 / 63卷
关键词
D O I
10.1107/S0907444906052024
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Crystallographers are increasingly determining structures of protein constructs that include His tags. Many have taken for granted that these tags have little effect on the native structure. This paper surveys and compares crystal structures with and without His tags. It is observed that actual refined tag residues fitted into density occur in less that 10% of the tagged sequences. However, higher resolution crystals are observed when this occurs. It is shown that these purification tags generally have no significant effect on the structure of the native protein. Resolution and R factors are not affected, but the overall B factors are slightly higher. Additional annotation in the PDB format to make tag definition explicit is suggested.
引用
收藏
页码:295 / 301
页数:7
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