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首页> 外文期刊>Crystal growth & design >Polymer-induced heteronucleation for protein single crystal growth: Structural elucidation of bovine liver catalase and concanavalin a forms
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Polymer-induced heteronucleation for protein single crystal growth: Structural elucidation of bovine liver catalase and concanavalin a forms

机译:聚合物诱导的蛋白质单晶生长异核:牛肝过氧化氢酶和伴刀豆球蛋白a形式的结构解析

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摘要

Obtaining single crystals for X-ray diffraction remains a major bottleneck in structural biology; when existing crystal growth methods fail to yield suitable crystals, often the target rather than the crystallization approach is reconsidered. Here we demonstrate that polymer-induced heteronucleation, a powerful technique that has been used for small molecule crystallization form discovery, can be applied to protein crystallization by optimizing the heteronucleant composition and crystallization formats for crystallizing a wide range of protein targets. Applying these advances to two benchmark proteins resulted in dramatically increased crystal size, enabling structure determination, for a half century old form of bovine liver catalase (BLC) that had previously only been characterized by electron microscopy, and the discovery of two new forms of concanavalin A (conA) from the Jack bean and accompanying structural elucidation of one of these forms.
机译:获得用于X射线衍射的单晶仍然是结构生物学的主要瓶颈。当现有的晶体生长方法无法产生合适的晶体时,通常会重新考虑目标而非结晶方法。在这里,我们证明了聚合物诱导的异核作用,一种已经用于小分子结晶形式发现的强大技术,可以通过优化异核物质的组成和结晶形式以使多种蛋白质靶物结晶,来应用于蛋白质结晶。将这些进展应用于两种基准蛋白可显着增加晶体尺寸,从而能够确定半个世纪以前仅通过电子显微镜表征的牛肝过氧化氢酶(BLC)的结构,并发现两种新型伴刀豆球蛋白来自Jack bean的A(conA)以及对这些形式之一的结构说明。

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