title: 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, β = 100.71°. The asymmetric unit was estimated to contain three molecules.
authors.affiliation: School of Biotechnology and Graduate School of Biochemistry, Yeungnam University, Gyeongsan, Republic of Korea.
authors.forename: Eun Kyoung
authors.initials: EK
authors.lastname: Seo
authors.forename: Tae Woo
authors.initials: TW
authors.lastname: Kim
authors.forename: Hyun Ho
authors.initials: HH
authors.lastname: Park
mesh_terms: D018797:Cell Cycle Proteins; D002850:Chromatography, Gel; D003460:Crystallization; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D009687:Nuclear Proteins / Q000737:chemistry*; D017434:Protein Structure, Tertiary
chemical_list: D018797:Cell Cycle Proteins; D004268:DNA-Binding Proteins; D009687:Nuclear Proteins; C490060:SYCP3 protein, human
keywords: coiled-coil domain; synaptonemal complex protein SCP3