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

SUBMITTER: Matsui T

PROVIDER: S-EPMC2334994 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature

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

Matsui Takuto T Nishimura Shinsuke S Kijima Kenichi K Kawasaki Yasushi Y Tashiro Fumio F Miura Shigetoshi S

Acta crystallographica. Section F, Structural biology and crystallization communications 20070414 Pt 5

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 trig ...[more]

PMID: 17565181

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