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

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, ? = 100.71°. The asymmetric unit was estimated to contain three molecules.

SUBMITTER: Seo EK

PROVIDER: S-EPMC3818053 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature

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

Seo Eun Kyoung EK Kim Tae Woo TW Park Hyun Ho HH

Acta crystallographica. Section F, Structural biology and crystallization communications 20131030 Pt 11

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 ...[more]

PMID: 24192369

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