Literature DB >> 2181148

Crystallization of the globular domain of histone H5.

V Graziano1, S E Gerchman, A J Wonacott, R M Sweet, J R Wells, S W White, V Ramakrishnan.   

Abstract

The globular domain of histone H1/H5 binds to the nucleosome and is crucial for the formation of chromatin higher order structure. We have expressed in Escherichia coli a gene that codes for the globular domain of H5. The protein produced in E. coli is functional in nucleosome binding assays. We have obtained crystals of the protein that diffract to beyond 2.5 A (1 A = 0.1 nm) resolution. The crystals are orthorhombic with unit cell dimensions of a = 80.1 A, b = 67.5 A and c = 38.0 A.

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Year:  1990        PMID: 2181148     DOI: 10.1016/0022-2836(90)90122-3

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  3 in total

1.  Cooperative binding of the globular domains of histones H1 and H5 to DNA.

Authors:  J O Thomas; C Rees; J T Finch
Journal:  Nucleic Acids Res       Date:  1992-01-25       Impact factor: 16.971

Review 2.  Multifunctionality of the linker histones: an emerging role for protein-protein interactions.

Authors:  Steven J McBryant; Xu Lu; Jeffrey C Hansen
Journal:  Cell Res       Date:  2010-03-23       Impact factor: 25.617

3.  Interaction of chromatin with a histone H1 containing swapped N- and C-terminal domains.

Authors:  Jordana B Hutchinson; Manjinder S Cheema; Jason Wang; Krystal Missiaen; Ron Finn; Rodrigo Gonzalez Romero; John P H Th'ng; Michael Hendzel; Juan Ausió
Journal:  Biosci Rep       Date:  2015-04-27       Impact factor: 3.840

  3 in total

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