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Projection Structure of Full Length Connexin 43 by Electron Cryo-Crystallography

机译：电子低温晶体学对全长连接蛋白43的投影结构

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We previously used electron cryo-crystallography to determine the three-dimensional structure of recombinant gap junction channels formed by a C-terminal truncation mutant of Cx43 (11). The dodecameric channel is formed by the end-to-end docking of two hexameric connexons, each comprised of 24 transmembrane α-helices. We have now generated two-dimensional crystals of the recombinant, full-length channel, as well as crystals in which the C-tail has been completely removed by trypsin digestion. Projection density maps at 7.5 A resolution closely resemble our previous analysis of the C-terminal truncation mutant (9). A difference map between the full length and trypsin-treated channels suggests that there are small but significant shifts in protein density upon removal of the C-tail.
机译：我们以前使用电子冷冻晶体学来确定由Cx43的C端截短突变体形成的重组间隙连接通道的三维结构（11）。十二聚体通道由两个六聚体连接体的端对端对接形成，每个六聚体连接体由24个跨膜α螺旋组成。现在，我们已经生成了重组全长通道的二维晶体，​​以及其中通过胰蛋白酶消化完全去除了C尾的晶体。 7.5 A分辨率下的投影密度图非常类似于我们之前对C端截短突变体的分析（9）。全长通道和胰蛋白酶处理通道之间的差异图表明，去除C尾后，蛋白质密度会有很小但明显的变化。

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