Open AccessExpression, crystallization and preliminary X‐ray crystallographic studies of SCP3 coiled‐coil domain
Author(s) -
Seo Eun Kyoung,
Kim Tae Woo,
Park Hyun Ho
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113026663
Subject(s) - crystallography , synaptonemal complex , crystallization , coiled coil , molecule , domain (mathematical analysis) , chemistry , homologous chromosome , biochemistry , organic chemistry , gene , mathematical analysis , mathematics
The synaptonemal complex protein SCP3 is one of the components of the lateral element of the synaptonemal complex, which is a meiosis‐specific complex structure formed at the synapse of homologous chromosomes. In this study, a C‐terminal coiled‐coil domain, SCP3, was overexpressed in Escherichia coli with an engineered C‐terminal His tag. The coiled‐coil domain of SCP3 was then purified to homogeneity and crystallized at 293 K. X‐ray diffraction data were collected to a resolution of 3.2 Å from a crystal belonging to space group C 2, with unit‐cell parameters a = 121.29, b = 43.08, c = 57.42 Å, β = 100.71°. The asymmetric unit was estimated to contain three molecules.