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

Eun Kyoung Seo, Tae Woo Kim, Hyun Ho Park

Research output: Contribution to journalArticle

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 languageEnglish
Pages (from-to)1281-1283
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume69
Issue number11
DOIs
Publication statusPublished - 2013 Nov

Keywords

  • Coiled-coil domain
  • Synaptonemal complex protein SCP3

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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