title: Crystallization and preliminary X-ray analysis of recombinant histone HPhA from the hyperthermophilic archaeon Pyrococcus horikoshii OT3.
abstract: Recombinant archaeal histone from the hyperthermophile Pyrococcus horikoshii OT3 (HPhA) was crystallized by the hanging-drop vapour-diffusion method. Crystals grew at 291 K in 200 mM (NH(4))(2)SO(4), 100 mM sodium acetate buffer pH 4.6, 19% PEG 4000. Diffraction data were obtained to a resolution of 2.3 A from a single frozen crystal, which belonged to space group P2(1) with unit-cell parameters a = 34.99, b = 46.89, c = 35.02 A, alpha = gamma = 90, beta = 104 degrees. The asymmetric unit contained two molecules and had a solvent content of approximately 35%.
authors.affiliation: Laboratory of Structural Biology, Department of Biological Science and Technology and MOE Laboratory of Protein Science, Tsinghua University, Beijing 100084, People's Republic of China.
authors.forename: Ti
authors.initials: T
authors.lastname: Li
authors.forename: Xin
authors.initials: X
authors.lastname: Ji
authors.forename: Fei
authors.initials: F
authors.lastname: Sun
authors.forename: Renjun
authors.initials: R
authors.lastname: Gao
authors.forename: Shugui
authors.initials: S
authors.lastname: Cao
authors.forename: Yan
authors.initials: Y
authors.lastname: Feng
authors.forename: Zihe
authors.initials: Z
authors.lastname: Rao
mesh_terms: D003460:Crystallization; D004926:Escherichia coli / Q000235:genetics; D006657:Histones / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D019711:Pyrococcus / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D014961:X-Ray Diffraction
chemical_list: D006657:Histones; D011994:Recombinant Proteins