Structure of pig heart citrate synthase at 1.78 A resolution.
Structure of pig heart citrate synthase at 1.78 A resolution.
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DOI：
10.1107/s1744309109008343
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发表时间：
2009-05
期刊：
影响因子：
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通讯作者：
S. Larson;J. Day;Chieugiang Nguyen;R. Cudney;A. McPherson
中科院分区：
文献类型：
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作者：
S. Larson;J. Day;Chieugiang Nguyen;R. Cudney;A. McPherson
猪心柠檬酸合酶是从含有胱胺二盐酸盐、苯甲酰胺和苯甲脒盐酸盐的小分子混合物中结晶出来的。使用同步加速器数据将结构精修至0.179的R因子（R（free）= 0.222），分辨率为1.78 A。该模型包括全长蛋白质、氯离子、硫酸根离子、305个水分子和通过二硫键连接到Cys184的意外部分，其被建模为通过与小分子混合物中的胱胺进行二硫键交换而产生的半胱胺分子。
Pig heart citrate synthase was crystallized from a small-molecule cocktail containing cystamine dihydrochloride, aspartame and benzamidine hydrochloride. The structure was refined to an R factor of 0.179 (R(free) = 0.222) using synchrotron data to a resolution of 1.78 A. The model includes the full-length protein, a chloride ion, a sulfate ion, 305 water molecules and an unexpected moiety attached through a disulfide linkage to Cys184, which was modeled as a half-cystamine molecule generated by disulfide exchange with the cystamine in the small-molecule cocktail.