Selenourea: a convenient phasing vehicle for macromolecular X-ray crystal structures.
Selenourea: a convenient phasing vehicle for macromolecular X-ray crystal structures.
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Selenourea：一种用于大分子X射线晶体结构的方便的相分化车辆。
DOI：
10.1038/srep37123
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发表时间：
2016-11-14
影响因子：
4.6
通讯作者：
Luo Z
中科院分区：
文献类型：
--
作者：
Luo Z
大多数新的蛋白质的X射线晶体结构是目前解决的异常衍射信号后，硒掺入硒代蛋氨酸代替天然蛋氨酸的基因工程方法提供的。然而，硒可以以硒化硒（SeC（NH2）2）的形式插入蛋白质晶体中，通过将硒化硒的结晶粉末添加到具有天然晶体的母液或冷冻溶液中，类似于重原子衍生化的经典程序。硒主要通过氢键与大分子表面的活性基团结合，其中硒原子可作为受体，酰胺基团可作为供体。硒具有不同于重原子试剂和卤素离子的化学性质，并提供了一种方便的方法来定相大分子的晶体结构。
Majority of novel X-ray crystal structures of proteins are currently solved using the anomalous diffraction signal provided by selenium after incorporation of selenomethionine instead of natural methionine by genetic engineering methods. However, selenium can be inserted into protein crystals in the form of selenourea (SeC(NH2)2), by adding the crystalline powder of selenourea into mother liquor or cryo-solution with native crystals, in analogy to the classic procedure of heavy-atom derivatization. Selenourea is able to bind to reactive groups at the surface of macromolecules primarily through hydrogen bonds, where the selenium atom may serve as acceptor and amide groups as donors. Selenourea has different chemical properties than heavy-atom reagents and halide ions and provides a convenient way of phasing crystal structures of macromolecules.