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人类联会复合体蛋白1卷曲螺旋结构域中部的X射线晶体学研究。

X-ray crystallographic studies of the middle part of the human synaptonemal complex protein 1 coiled-coil domain.

作者信息

Park Hyun Ho

机构信息

Department of Biochemistry, Yeungnam University, Gyeongsan, Republic of Korea.

出版信息

Acta Crystallogr F Struct Biol Commun. 2015 Sep;71(Pt 9):1131-4. doi: 10.1107/S2053230X15012728. Epub 2015 Aug 25.

Abstract

The synaptonemal complex is a meiosis-specific complex structure formed at the synapse of homologous chromosomes to hold them together during meiosis. Synaptonemal complex protein 1 (SYCP1) is one of the components of the syneptonemal complex. In this study, the short form of the coiled-coil domain of SYCP1 was overexpressed in Escherichia coli with an engineered C-terminal His tag. The short form of the coiled-coil domain of SYCP1 was then purified to homogeneity and crystallized at 293 K. X-ray diffraction data were collected to a resolution of 3.0 Å from a crystal belonging to space group I4, with unit-cell parameters a = 41.95, b = 41.95, c = 318.78 Å. The asymmetric unit was estimated to contain two molecules.

摘要

联会复合体是一种在减数分裂过程中于同源染色体突触处形成的特定于减数分裂的复杂结构,用于在减数分裂期间将同源染色体聚集在一起。联会复合体蛋白1(SYCP1)是联会复合体的组成成分之一。在本研究中,带有工程化C末端His标签的SYCP1卷曲螺旋结构域的短形式在大肠杆菌中过表达。然后将SYCP1卷曲螺旋结构域的短形式纯化至同质,并在293K下结晶。从属于空间群I4的晶体收集了分辨率为3.0 Å的X射线衍射数据,晶胞参数a = 41.95,b = 41.95,c = 318.78 Å。估计不对称单位包含两个分子。

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