Open AccessCrystallization and preliminary X‐ray diffraction data of the rat histone H1 0 globular domain
Author(s) -
Matsui Takuto,
Nishimura Shinsuke,
Kijima Kenichi,
Kawasaki Yasushi,
Tashiro Fumio,
Miura Shigetoshi
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107015357
Subject(s) - crystallography , crystallization , chromatin , linker , histone h1 , histone , nucleosome , x ray crystallography , chemistry , dna , materials science , biophysics , diffraction , biology , biochemistry , physics , organic chemistry , optics , computer science , operating system
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 H1 0 , 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 P 3 1 21, 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 Å 3 Da −1 and 59.6%, respectively.