Open AccessPurification, crystallization and preliminary X‐ray diffraction analysis of the histone chaperone cia1 from fission yeast
Author(s) -
Umehara Takashi,
Otta Yumi,
Tsuganezawa Keiko,
Matsumoto Takehisa,
Tanaka Akiko,
Horikoshi Masami,
Padmanabhan Balasundaram,
Yokoyama Shigeyuki
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105030927
Subject(s) - crystallography , schizosaccharomyces pombe , yeast , histone , chaperone (clinical) , nucleosome , crystallization , monoclinic crystal system , escherichia coli , saccharomyces cerevisiae , chemistry , biology , biophysics , crystal structure , biochemistry , gene , medicine , pathology , organic chemistry
In fission yeast, cia1 + is an essential gene that encodes a histone chaperone, a homologue of human CIA (CCG1‐interacting factor A) and budding yeast Asf1p (anti‐silencing function‐1), which both facilitate nucleosome assembly by interacting with the core histones H3/H4. The conserved domain (residues 1–161) of the cia1 + ‐encoded protein was expressed in Escherichia coli , purified to near‐homogeneity and crystallized by the sitting‐drop vapour‐diffusion method. The protein was crystallized in the monoclinic space group C 2, with unit‐cell parameters a = 79.16, b = 40.53, c = 69.79 Å, β = 115.93° and one molecule per asymmetric unit. The crystal diffracted to beyond 2.10 Å resolution using synchrotron radiation.