...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Affinity tags can reduce merohedral twinning of membrane protein crystals.
【24h】

Affinity tags can reduce merohedral twinning of membrane protein crystals.

机译：亲和标签可以减少缺面的双晶膜蛋白晶体。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

This work presents a comparison of the crystal packing of three eukaryotic membrane proteins: human aquaporin 1, human aquaporin 5 and a spinach plasma membrane aquaporin. All were purified from expression constructs both with and without affinity tags. With the exception of tagged aquaporin 1, all constructs yielded crystals. Two significant effects of the affinity tags were observed: crystals containing a tag typically diffracted to lower resolution than those from constructs encoding the protein sequence alone and constructs without a tag frequently produced crystals that suffered from merohedral twinning. Twinning is a challenging crystallographic problem that can seriously hinder solution of the structure. Thus, for integral membrane proteins, the addition of an affinity tag may help to disrupt the approximate symmetry of the protein and thereby reduce or avoid merohedral twinning.
机译：这项工作提出了一种比较的晶体包装三个真核膜蛋白:水通道蛋白1,人类和水通道蛋白5菠菜等离子体膜水通道蛋白。从表达式构造与和净化没有亲和力标签。标记水通道蛋白1,构造了晶体。标记观察:晶体包含一个标记通常衍射分辨率低于编码蛋白的结构没有一个标签序列,构造经常遭受产生晶体缺面的双晶。晶体会严重的问题影响结构的解决方案。完整的膜蛋白,添加一个亲和标签有助于扰乱近似对称的蛋白质,从而减少或避免缺面的双晶。

著录项

相似文献

  • 外文文献
  • 中文文献
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号