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Acta Crystallogr Sect F Struct Biol Cryst Commun. May 1, 2007; 63(Pt 5): 403–405.
Published online Apr 14, 2007. doi:  10.1107/S1744309107015357
PMCID: PMC2334994

Crystallization and preliminary X-ray diffraction data of the rat histone H10 globular domain

Abstract

The linker histones H1 are a family of lysine-rich proteins that associate with the stretch of DNA that enters and exits the nucleosome. The linker histones facilitate the compaction and condensation of chromatin. The globular domain of histone H10, a specific subtype of histone H1, was crystallized at 288 K using the microbatch under silicone oil method with potassium phosphate as a precipitating agent. Diffraction data were collected to a resolution of 1.98 Å. The crystal belongs to the trigonal space group P3121, with unit-cell parameters a = 54.13, b = 54.13, c = 71.99 Å, and contains one molecule per asymmetric unit. The V M value and solvent content were calculated to be 3.04 Å3 Da−1 and 59.6%, respectively.

Keywords: histone H10

Articles from Acta Crystallographica Section F: Structural Biology and Crystallization Communications are provided here courtesy of International Union of Crystallography