Crystallization and preliminary X-ray analysis of TBP-interacting protein from the hyperthermophilic archaeon Thermococcus kodakaraensis strain KOD1.
The 26 kDa TBP (TATA-binding protein) interacting protein from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 (Tk-TIP26) is a possible transcriptional regulatory protein in Thermococcales. Here, the crystallization of both the native and selenomethionine-substituted proteins and data collection are described. The native crystals belong to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = 73.83, c = 86.41 A, and diffract to 2.2 A using synchrotron radiation. MAD data was collected and a Bijvoet difference Patterson map showed strong peaks sufficient to determine the positions of the Se atoms.
Yamamoto
Takahiko
T
Department of Materials Chemistry, Graduate School of Engineering, Osaka University, Yamada-oka 2-1, Suita, Osaka 565-0871, Japan.
Matsuda
Tomoki
T
Sakamoto
Nami
N
Matsumura
Hiroyoshi
H
Inoue
Tsuyoshi
T
Morikawa
Masaaki
M
Kanaya
Shigenori
S
Kai
Yasushi
Y
D019843:Archaeal Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D004926:Escherichia coli / Q000235:genetics; D012645:Selenomethionine / Q000737:chemistry; D017356:Synchrotrons; D035181:TATA-Box Binding Protein / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D019712:Thermococcus / Q000737:chemistry* / Q000235:genetics
D019843:Archaeal Proteins; D035181:TATA-Box Binding Protein; D012645:Selenomethionine