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Crystallization and preliminary X-ray study of AMP nucleosidase.

Adenosine-5'-monophosphate nucleosidase from Escherichia coli has been crystallized in the presence of its strong competitive inhibitor formycin 5'-monophosphate and its allosteric activator adenosine 5'-triphosphate. Crystals are tetragonal bipyramids which grow to 1.2 mm in the longest dimension, are resistant to radiation damage, and diffract to a resolution of 3.5 A. The space group is P4(1)2(1)2 or P4(3)2(1)2, and the unit cell dimensions are a = 120.1 A and c = 243.7 A. The asymmetric unit is estimated to contain four subunits of 52,000 daltons. The crystals appear suitable for single crystal x-ray structure investigation.[1]


  1. Crystallization and preliminary X-ray study of AMP nucleosidase. Giranda, V.L., Berman, H.M., Schramm, V.L. J. Biol. Chem. (1986) [Pubmed]
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