title: Crystallization of the globular domain of histone H5.
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.
authors.affiliation: Biology Department, Brookhaven National Laboratory, Upton, NY 11973.
authors.forename: V
authors.initials: V
authors.lastname: Graziano
authors.forename: S E
authors.initials: SE
authors.lastname: Gerchman
authors.forename: A J
authors.initials: AJ
authors.lastname: Wonacott
authors.forename: R M
authors.initials: RM
authors.lastname: Sweet
authors.forename: J R
authors.initials: JR
authors.lastname: Wells
authors.forename: S W
authors.initials: SW
authors.lastname: White
authors.forename: V
authors.initials: V
authors.lastname: Ramakrishnan
mesh_terms: D003460:Crystallization; D004926:Escherichia coli / Q000235:genetics*; D015870:Gene Expression; D006657:Histones / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D009707:Nucleosomes / Q000378:metabolism; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D006657:Histones; D009707:Nucleosomes