Purification, crystallization and preliminary X-ray diffraction analysis of the histone chaperone cia1 from fission yeast

Journal Article · Tue Nov 01 04:00:00 EST 2005 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309105030927· OSTI ID:22356171

Umehara, Takashi; Otta, Yumi; Tsuganezawa, Keiko; Matsumoto, Takehisa; Tanaka, Akiko ^[1]; Horikoshi, Masami ^[2]; Padmanabhan, Balasundaram ^[1]; Yokoyama, Shigeyuki ^[1]

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1. RIKEN Genomic Sciences Center, 1-7-22 Suehiro, Tsurumi, Yokohama 230-0045 (Japan)
2. Laboratory of Developmental Biology, Institute of Molecular and Cellular Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 111-0032 (Japan)

The histone chaperone cia1 from fission yeast has been overexpressed in E. coli, purified and crystallized using the vapour-diffusion method. In fission yeast, cia1{sup +} 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{sup +}-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 C2, 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.

• OSTI ID: 22356171
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 11 Vol. 61; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
CRYSTALS
DIFFUSION
ESCHERICHIA COLI
MOLECULES
RESOLUTION
SPACE GROUPS
SYNCHROTRON RADIATION
X-RAY DIFFRACTION