Open AccessCrystallization and preliminary X‐ray crystallographic analysis of a conserved domain in plants and prokaryotes from Pyrococcus horikoshii OT3
Author(s) -
Lin Linyen,
Nakano Hiroaki,
Uchiyama Susumu,
Fujimoto Satoru,
Ohkubo Tadayasu,
Matsunaga Sachihiro,
Nakamura Shota,
Kobayashi Yuji,
Fukui Kiichi
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105007815
Subject(s) - pyrococcus horikoshii , crystallography , crystallization , chemistry , crystal structure , organic chemistry
A plant‐ and prokaryote‐conserved domain (PPC) has previously been found in AT‐hook motif nuclear localized protein 1 (AHL1) localized in the nuclear matrix of Arabidopsis thaliana ( At AHL1). At AHL1 has a DNA‐binding function. Mutation analyses of At AHL1 has previously revealed that the hydrophobic region of the PPC domain is essential for its nuclear localization. In this study, the PPC of the hyperthermophilic archaebacterium Pyrococcus horikoshii ( Ph PPC) was crystallized using the hanging‐drop vapour‐diffusion method. The crystals belonged to the hexagonal space group P 6 3 22, with unit‐cell parameters a = b = 53.69, c = 159.2 Å. Data were obtained at 100 K, with diffraction being observed to a resolution of 1.7 Å. A complete data set from crystals of the SeMet‐substituted protein was also obtained.