Purification, crystallization and preliminary X-ray analysis of Methanococcus jannaschii TATA box-binding protein (TBP).
TATA box-binding protein (TBP) from Methanococcus jannaschii has been crystallized by the hanging-drop vapour-diffusion method using PEG MME 2000 as a precipitant. The crystal belongs to space group P21, with unit-cell parameters a = 53.2, b = 55.5, c = 123.4 A,a = 90.0, fi = 91.0, y = 90.0 degrees, and contains four molecules in the asymmetric unit. A data set was collected to 1.9 A resolution using synchrotron radiation. A molecular-replacement solution was found using the structure of TBP from Sulfolobus acidocaldarius as a model. Crystallographic refinement is in progress.
Adachi
Naruhiko
N
Institute of Molecular and Cellullar Biosciences, The University of Tokyo, Tokyo, Japan.
Natsume
Ryo
R
Senda
Miki
M
Muto
Shinsuke
S
Senda
Toshiya
T
Horikoshi
Masai
M
D000595:Amino Acid Sequence; D000818:Animals; D018360:Crystallography, X-Ray; D004058:Diffusion; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D017017:Methanococcus / Q000378:metabolism*; D008969:Molecular Sequence Data; D010802:Phylogeny; D010957:Plasmids / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D016945:Sulfolobus acidocaldarius / Q000378:metabolism; D035181:TATA-Box Binding Protein / Q000737:chemistry*; D013696:Temperature; D014961:X-Ray Diffraction
D035181:TATA-Box Binding Protein