Crystallization and preliminary X-ray diffraction data of the rat histone H1(0) globular domain.

Acta Crystallogr Sect F Struct Biol Cryst Commun

Department of Biological Science and Technology, Tokyo University of Science, Noda, Chiba 278-8510, Japan.

Published: May 2007

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 A. The crystal belongs to the trigonal space group P3(1)21, with unit-cell parameters a = 54.13, b = 54.13, c = 71.99 A, and contains one molecule per asymmetric unit. The V(M) value and solvent content were calculated to be 3.04 A3 Da(-1) and 59.6%, respectively.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2334994PMC
http://dx.doi.org/10.1107/S1744309107015357DOI Listing

Publication Analysis

Top Keywords

diffraction data
8
histone h10
8
globular domain
8
linker histones
8
crystallization preliminary
4
preliminary x-ray
4
x-ray diffraction
4
data rat
4
rat histone
4
h10 globular
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!