Related Experiment Video
Updated: May 6, 2026

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
Published on: January 6, 2017
Expression, crystallization and preliminary X-ray crystallographic studies of SCP3 coiled-coil domain
Eun Kyoung Seo1, Tae Woo Kim, Hyun Ho Park
1School of Biotechnology and Graduate School of Biochemistry, Yeungnam University, Gyeongsan, Republic of Korea.
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.
More Related Videos
09:15Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
Published on: January 10, 2018
09:31PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase
Published on: September 26, 2020