Expression, purification, crystallization and preliminary crystallographic study of the SRA domain of the human UHRF1 protein

摘要

The SET- and RING finger-associated (SRA) domain of human UHRF1 protein has been overexpressed in E. coli, purified and crystallized. The three-dimensional structure of the protein in its SeMet form was solved from 2.2 Å diffraction data using the multiple anomalous dispersion method.