skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

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

Abstract

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.

Authors:
; ; ; ;  [1];  [2];  [3];  [1];  [1];  [4];  [4]
  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)
  3. (ERATO), Japan Science and Technology Corporation (JST), 5-9-6 Tokodai, Tsukuba, Ibaraki 300-2635 (Japan)
  4. (Japan)
Publication Date:
OSTI Identifier:
22356171
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 61; Journal Issue: Pt 11; Other Information: PMCID: PMC1978123; PMID: 16511210; PUBLISHER-ID: pu5100; OAI: oai:pubmedcentral.nih.gov:1978123; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; DIFFUSION; ESCHERICHIA COLI; MOLECULES; RESOLUTION; SPACE GROUPS; SYNCHROTRON RADIATION; X-RAY DIFFRACTION

Citation Formats

Umehara, Takashi, Otta, Yumi, Tsuganezawa, Keiko, Matsumoto, Takehisa, Tanaka, Akiko, Horikoshi, Masami, Horikoshi Gene Selector Project, Exploratory Research for Advanced Technology, Padmanabhan, Balasundaram, E-mail: paddy@gsc.riken.jp, Yokoyama, Shigeyuki, E-mail: paddy@gsc.riken.jp, RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo, Hyogo 679-5148, and Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033. Purification, crystallization and preliminary X-ray diffraction analysis of the histone chaperone cia1 from fission yeast. United Kingdom: N. p., 2005. Web. doi:10.1107/S1744309105030927.
Umehara, Takashi, Otta, Yumi, Tsuganezawa, Keiko, Matsumoto, Takehisa, Tanaka, Akiko, Horikoshi, Masami, Horikoshi Gene Selector Project, Exploratory Research for Advanced Technology, Padmanabhan, Balasundaram, E-mail: paddy@gsc.riken.jp, Yokoyama, Shigeyuki, E-mail: paddy@gsc.riken.jp, RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo, Hyogo 679-5148, & Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033. Purification, crystallization and preliminary X-ray diffraction analysis of the histone chaperone cia1 from fission yeast. United Kingdom. doi:10.1107/S1744309105030927.
Umehara, Takashi, Otta, Yumi, Tsuganezawa, Keiko, Matsumoto, Takehisa, Tanaka, Akiko, Horikoshi, Masami, Horikoshi Gene Selector Project, Exploratory Research for Advanced Technology, Padmanabhan, Balasundaram, E-mail: paddy@gsc.riken.jp, Yokoyama, Shigeyuki, E-mail: paddy@gsc.riken.jp, RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo, Hyogo 679-5148, and Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033. Tue . "Purification, crystallization and preliminary X-ray diffraction analysis of the histone chaperone cia1 from fission yeast". United Kingdom. doi:10.1107/S1744309105030927.
@article{osti_22356171,
title = {Purification, crystallization and preliminary X-ray diffraction analysis of the histone chaperone cia1 from fission yeast},
author = {Umehara, Takashi and Otta, Yumi and Tsuganezawa, Keiko and Matsumoto, Takehisa and Tanaka, Akiko and Horikoshi, Masami and Horikoshi Gene Selector Project, Exploratory Research for Advanced Technology and Padmanabhan, Balasundaram, E-mail: paddy@gsc.riken.jp and Yokoyama, Shigeyuki, E-mail: paddy@gsc.riken.jp and RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo, Hyogo 679-5148 and Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033},
abstractNote = {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.},
doi = {10.1107/S1744309105030927},
journal = {Acta Crystallographica. Section F},
number = Pt 11,
volume = 61,
place = {United Kingdom},
year = {Tue Nov 01 00:00:00 EST 2005},
month = {Tue Nov 01 00:00:00 EST 2005}
}