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X‐ray crystallographic studies of the middle part of the human synaptonemal complex protein 1 coiled‐coil domain
Author(s) -
Park Hyun Ho
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15012728
Subject(s) - synaptonemal complex , coiled coil , homologous chromosome , meiosis , crystallography , biology , microbiology and biotechnology , chemistry , genetics , gene
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 I 4, with unit‐cell parameters a = 41.95, b = 41.95, c = 318.78 Å. The asymmetric unit was estimated to contain two molecules.