Open AccessCrystallization and preliminary X‐ray crystallographic studies of casein kinase I‐like protein from rice
Author(s) -
Do Kyoung Hun,
Park Hyun Ho
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112000474
Subject(s) - protein kinase a , threonine , crystallography , kinase , cytokinesis , casein kinase 2 , protein kinase domain , crystallization , chemistry , biochemistry , casein kinase 1 , biology , serine , microbiology and biotechnology , biophysics , cell division , cell , phosphorylation , cyclin dependent kinase 2 , gene , organic chemistry , mutant
Casein kinase I (CKI) is a serine/threonine protein kinase that performs various functions in the cell, such as DNA repair, cell‐cycle regulation, cytokinesis, vesicular trafficking, morphogenesis and circadian‐rhythm regulation. CKI proteins contain a highly conserved catalytic domain at the N‐terminus and a highly diverse regulatory domain that is responsible for substrate specificity at the C‐terminus. In this study, CKI from rice (riceCKI) was overexpressed in Escherichia coli with an engineered C‐terminal His tag. RiceCKI was then purified to homogeneity and crystallized at 293 K. X‐ray diffraction data were collected to a resolution of 2.0 Å from a crystal belonging to the monoclinic space group C 2, with unit‐cell parameters a = 108.83, b = 69.60, c = 55.85 Å, β = 109.47°. The asymmetric unit was estimated to contain one monomer.