Purification, crystallization and preliminary X-ray analysis of two nudix hydrolases from Deinococcus radiodurans.
Two nudix hydrolases from Deinococcus radiodurans have been purified and crystallized. Diffraction data have been collected to 1.4 and 1.9 A resolution for DR1025 and DR0079, respectively. DR1025 belongs to space group P4(1)2(1)2/P4(3)2(1)2, with unit-cell parameters a = b = 53.2, c = 122.6 A (unit-cell Volume 346 883 A(3), V(M) = 2.5 A(3) Da(-1), solvent content 50.2%). DR0079 belongs to space group C222(1), with unit-cell parameters a = 34.1, b = 157.2, c = 126.5 A (unit-cell Volume 677 308 A(3), V(M) = 2.2 A(3) Da(-1), solvent content 44.0%). The calculated cell content of DR1025 indicates the presence of one molecule in the asymmetric unit. Dynamic light scattering and gel filtration suggest it to be a dimer in solution. The space group and unit-cell parameters of DR0079 indicate the presence of two molecules per asymmetric unit. Gel filtration and NMR spectroscopy suggest it to be a monomer in solution.
Holbrook
Elizabeth Litzenberger
EL
Structural Biology Department, Lawrence Berkeley National Laboratory, CA 94720, USA.
Schulze-Gahmen
Ursula
U
Buchko
Garry W
GW
Ni
Shuisong
S
Kennedy
Michael A
MA
Holbrook
Stephen R
SR
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D034301:Deinococcus / Q000201:enzymology*; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry; D008027:Light; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry; D011755:Pyrophosphatases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D012542:Scattering, Radiation; D000096964:Nudix Hydrolases
D029968:Escherichia coli Proteins; D010744:Phosphoric Monoester Hydrolases; D011755:Pyrophosphatases; D000096964:Nudix Hydrolases; C052211:mutT protein, E coli