Comparative analysis of amino acids and amino-acid derivatives in protein crystallization

被引:14
作者
Ito, Len [1 ,2 ]
Shiraki, Kentaro [3 ]
Yamaguchi, Hiroshi [2 ]
机构
[1] Japan Synchrotron Radiat Res Inst SPring 8, Sayo, Hyogo 6795198, Japan
[2] Kwansei Gakuin Univ, Sch Sci & Technol, Sanda, Hyogo 6691337, Japan
[3] Univ Tsukuba, Inst Appl Phys, Tsukuba, Ibaraki 3058573, Japan
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2010年 / 66卷
关键词
DYNAMIC LIGHT-SCATTERING; EGG-WHITE LYSOZYME; CRYSTAL-GROWTH; THERMAL INACTIVATION; AGGREGATION; MACROMOLECULES; NUCLEATION; STRATEGY; ARGININE;
D O I
10.1107/S1744309110013710
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Optimal conditions for protein crystallization are difficult to determine because proteins tend to aggregate in saturated solutions. This study comprehensively evaluates amino acids and amino-acid derivatives as additives for crystallization. This fourth component of the solution increases the probability of crystallization of hen egg-white lysozyme in various precipitants owing to a decrease in aggregation. These results suggest that the addition of certain types of amino acids and amino-acid derivatives, such as Arg, Lys and esterified and amidated amino acids, is a simple method of improving the success rate of protein crystallization.
引用
收藏
页码:744 / 749
页数:6
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