Crystallization and preliminary X-ray diffraction studies on the mutT nucleoside triphosphate pyrophosphohydrolase of Escherichia coli.
The mutT nucleoside triphosphatase, which prevents AT----CG transversions during DNA replication, has been crystallized from ammonium sulfate utilizing a novel technique involving vapor diffusion in capillaries. X-ray diffraction analysis has revealed that the crystals are monoclinic, space group P2(1), with cell constants a = 34.14, b = 72.54, c = 56.38, and beta = 98.90. The Vm value of 2.31 A3/Da is consistent with two molecules of enzyme per asymmetric unit. The crystals are reasonably stable in the x-ray beam, and a data set to 2.5 A resolution has been collected for native protein. There is evidence that the crystals diffract to at least 2.1 A.
Bessman
M J
MJ
McCollum-Pratt Institute, Baltimore, Maryland.
Bullions
L C
LC
Bhatnagar
S K
SK
Braden
B C
BC
Love
W E
WE
D003461:Crystallography; D004926:Escherichia coli / Q000201:enzymology*; D043583:Nucleoside-Triphosphatase; D010744:Phosphoric Monoester Hydrolases / Q000648:ultrastructure*; D011487:Protein Conformation; D011755:Pyrophosphatases / Q000648:ultrastructure*; D014961:X-Ray Diffraction
D010744:Phosphoric Monoester Hydrolases; D011755:Pyrophosphatases; D043583:Nucleoside-Triphosphatase