Outer membrane proteins are structurally distinct from those that reside in the inner membrane and play important roles in bacterial pathogenicity and human metabolism. X-ray crystallography studies on >40 different outer membrane proteins have revealed that the transmembrane portion of these proteins can be constructed from either beta-sheets or less commonly from alpha-helices. The most common architecture is the beta-barrel, which can be formed from either a single anti-parallel sheet, fused at both ends to form a barrel or from multiple peptide chains. Outer membrane proteins exhibit considerable rigidity and stability, making their study through x-ray crystallography particularly tractable. As the number of structures of outer membrane proteins increases a more rational approach to their crystallization can be made. Herein we analyse the crystallization data from 53 outer membrane proteins and compare the results to those obtained for inner membrane proteins. A targeted sparse matrix screen for outer membrane protein crystallization is presented based on the present analysis.

中文翻译：

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深入了解外膜蛋白结晶。

外膜蛋白在结构上与内膜蛋白不同，在细菌致病性和人体代谢中起重要作用。对 > 40 种不同外膜蛋白的 X 射线晶体学研究表明，这些蛋白质的跨膜部分可以由β-折叠或不太常见的α-螺旋构成。最常见的结构是β-桶，它可以由单个反平行片形成，两端融合形成桶，也可以由多个肽链形成。外膜蛋白表现出相当大的刚性和稳定性，使它们通过 X 射线晶体学的研究特别容易处理。随着外膜蛋白结构数量的增加，可以对它们的结晶进行更合理的方法。在这里，我们分析了 53 种外膜蛋白的结晶数据，并将结果与​​内膜蛋白的结果进行了比较。基于本分析提出了用于外膜蛋白结晶的有针对性的稀疏矩阵筛选。