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.

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