Crystallization and preliminary X-ray crystallographic analysis of a conserved domain in plants and prokaryotes from Pyrococcus horikoshii OT3.
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 (AtAHL1). AtAHL1 has a DNA-binding function. Mutation analyses of AtAHL1 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 (PhPPC) was crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to the hexagonal space group P6(3)22, with unit-cell parameters a = b = 53.69, c = 159.2 A. Data were obtained at 100 K, with diffraction being observed to a resolution of 1.7 A. A complete data set from crystals of the SeMet-substituted protein was also obtained.
Lin
Linyen
L
Department of Biotechnology, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, 565-0871 Osaka, Japan.
Nakano
Hiroaki
H
Uchiyama
Susumu
S
Fujimoto
Satoru
S
Matsunaga
Sachihiro
S
Nakamura
Shota
S
Kobayashi
Yuji
Y
Ohkubo
Tadayasu
T
Fukui
Kiichi
K
D020816:Amino Acid Motifs; D029681:Arabidopsis Proteins / Q000737:chemistry*; D017124:Conserved Sequence; D003460:Crystallization / Q000379:methods; D004268:DNA-Binding Proteins / Q000737:chemistry*; D010944:Plants / Q000737:chemistry; D011387:Prokaryotic Cells / Q000737:chemistry; D043902:Pyrococcus horikoshii / Q000737:chemistry*; D012645:Selenomethionine; D014961:X-Ray Diffraction
C496143:AHL1 protein, Arabidopsis; D029681:Arabidopsis Proteins; D004268:DNA-Binding Proteins; D012645:Selenomethionine