Reference - PMID:16511210 - Purification, crystallization and preliminary X-ray diffraction analysis of the histone chaperone cia1 from fission yeast.
Reference summary
- PubMed ID
- PMID:16511210
- Title
- Purification, crystallization and preliminary X-ray diffraction analysis of the histone chaperone cia1 from fission yeast.
- Authors
- Umehara T, Otta Y, Tsuganezawa K, Matsumoto T, Tanaka A, Horikoshi M, Padmanabhan B, Yokoyama S
- Citation
- Acta Crystallogr Sect F Struct Biol Cryst Commun 2005 Nov 01;61(Pt 11):971-3
- Publication year
- 2005
- 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.
