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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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.[1]

References

  1. Crystallization and preliminary X-ray diffraction studies on the mutT nucleoside triphosphate pyrophosphohydrolase of Escherichia coli. Bessman, M.J., Bullions, L.C., Bhatnagar, S.K., Braden, B.C., Love, W.E. J. Biol. Chem. (1991) [Pubmed]
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