Abstract
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 293K. X-ray diffraction data were collected to a resolution of 3.2Å from a crystal belonging to space group C2, with unit-cell parameters a = 121.29, b = 43.08, c = 57.42Å, β = 100.71°. The asymmetric unit was estimated to contain three molecules.
Original language | English |
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Pages (from-to) | 1281-1283 |
Number of pages | 3 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 69 |
Issue number | 11 |
DOIs | |
Publication status | Published - 2013 Nov |
Keywords
- Coiled-coil domain
- Synaptonemal complex protein SCP3
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics