Literature DB >> 24192369

Expression, crystallization and preliminary X-ray crystallographic studies of SCP3 coiled-coil domain.

Eun Kyoung Seo1, Tae Woo Kim, Hyun Ho Park.   

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 293 K. X-ray diffraction data were collected to a resolution of 3.2 Å from a crystal belonging to space group C2, 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.

Entities:  

Keywords:  coiled-coil domain; synaptonemal complex protein SCP3

Mesh:

Substances:

Year:  2013        PMID: 24192369      PMCID: PMC3818053          DOI: 10.1107/S1744309113026663

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


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