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

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Takashi UmeharaShigeyuki Yokoyama

Abstract

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 C2, with unit-cell parameters a = 79.16, b = 40.53, c = 69.79 A, beta = 115.93 degrees and one molecule per asymmetric unit. The crystal diffracted to beyond 2.10 A resolution using synchrotron radiation.

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Citations

Jul 6, 2010·Protein Expression and Purification·Masatoshi WakamoriShigeyuki Yokoyama
Mar 13, 2008·The Journal of Biological Chemistry·Ali D MalayShigeyuki Yokoyama

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