首页> 外文期刊>Acta Crystallographica Section F >Cloning, purification, crystallization and preliminary crystallographic analysis of the tandem tudor domain of Sgf29 from Saccharomyces cerevisiae
【24h】

Cloning, purification, crystallization and preliminary crystallographic analysis of the tandem tudor domain of Sgf29 from Saccharomyces cerevisiae

机译:酿酒酵母Sgf29串联Tudor结构域的克隆,纯化,结晶和初步晶体学分析

获取原文
获取原文并翻译 | 示例
           

摘要

The protein Sgf29 has been identified as a subunit of the SAGA (Spt–Ada–Gcn5 acetyltransferase) histone acetyltransferase complex in Saccharomyces cerevisiae, which is conserved from yeast to humans. The tandem tudor domain at the C-terminus of Sgf29 was crystallized using the hanging-drop vapour-diffusion method and the crystals diffracted to 1.92 Å resolution. The crystals belonged to space group P212121, with unit-cell parameters a = 49.76, b = 95.10, c = 114.43 Å, and are estimated to contain one protein molecule per asymmetric unit.
机译:Sgf29蛋白已被鉴定为酿酒酵母中SAGA(Spt–Ada–Gcn5乙酰基转移酶)组蛋白乙酰基转移酶复合物的一个亚基,从酵母到人都是保守的。 Sgf29的C端的串联tudor域使用悬滴蒸气扩散法结晶,并且晶体衍射到1.92Å的分辨率。晶体属于空间群P2 1 2 1 2 1 ,单位晶胞参数a = 49.76,b = 95.10,c = 114.43 ,估计每个不对称单位包含一个蛋白质分子。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
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