Electron crystallography of macromolecular periodic arrays on phospholipid monolayers

Wah Chiu, Agustin J. Avila-Sakar , Michael F. Schmid
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引用次数: 33

Abstract

Electron crystallography has the potential of yielding structural information equivalent to x-ray diffraction. The major difficulty has been preparing specimens with the required structural order and size for diffraction and imaging in the electron microscope. 2D crystallization on phospholipid monolayers is capable of fulfilling both of these requirements. Crystals can form as a result of specific interactions with a protein's ligand or an analog, suitably linked to a lipid tail; or on a surface of complementary head-group charge. With such choices, the availability of a suitable lipid is limited only by synthetic chemistry. Ultimately, it is the quality and regularity of the protein-protein interactions that determine the crystalline order, as it is with any protein crystal. In the case of streptavidin, the monolayer crystal diffracts beyond 2.5 Å. A 3 Å projection map reconstructed from electron diffraction amplitudes and phases from images shows density which can be interpreted as β-sheets and clusters of side chains. It remains to be shown that the monolayer crystals are flat and diffract as well at high tilt angle as untilted. Technological issues such as charging must be resolved. With parallel advances in data collection and processing, electron crystallography of monolayer macromolecular crystals will eventually take its place beside x-ray crystallography and NMR as a routine and efficient structural technique.

磷脂单层上大分子周期阵列的电子晶体学研究
电子晶体学具有产生相当于x射线衍射的结构信息的潜力。主要的困难是制备具有衍射和电子显微镜成像所需的结构顺序和尺寸的样品。磷脂单分子层上的二维结晶能够满足这两个要求。晶体可以通过与蛋白质配体或类似物的特定相互作用形成,适当地与脂质尾部相连;或者在互补头基电荷的表面上。有了这样的选择,合适的脂质的可用性只受合成化学的限制。最终,蛋白质之间相互作用的质量和规律决定了晶体的顺序,就像任何蛋白质晶体一样。在链亲和素的情况下,单层晶体衍射超过2.5 Å。从电子衍射振幅和相位重建的3 Å投影图显示密度,可以解释为β-片和侧链簇。有待证明的是,单层晶体是平坦的,在高倾斜角度和倾斜角度下也能衍射。充电等技术问题必须得到解决。随着数据收集和处理的平行发展,单层大分子晶体的电子晶体学将最终取代x射线晶体学和核磁共振作为常规和有效的结构技术。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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