Crystallization and preliminary X-ray crystallographic studies of casein kinase I-like protein from rice

Title
Crystallization and preliminary X-ray crystallographic studies of casein kinase I-like protein from rice
Author(s)
박현호도경훈[도경훈]
Keywords
PHOSPHORYLATION
Issue Date
201203
Publisher
WILEY-BLACKWELL
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, v.68, pp.298 - 300
Abstract
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 angstrom from a crystal belonging to the monoclinic space group C2, with unit-cell parameters a = 108.83, b = 69.60, c = 55.85 angstrom, beta = 109.47 degrees. The asymmetric unit was estimated to contain one monomer.
URI
http://hdl.handle.net/YU.REPOSITORY/29516http://dx.doi.org/10.1107/S1744309112000474
ISSN
1744-3091
Appears in Collections:
이과대학 > 화학생화학부 > Articles
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE