Crystallization and preliminary X-ray study of AMP nucleosidase

V. L. Giranda, H. M. Berman, V. L. Schramm

Research output: Contribution to journalArticle

4 Scopus citations

Abstract

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 Å. The space group is P41212 or P43212, and the unit cell dimensions are a = 120.1 Å and c = 243.7 Å. The asymmetric unit is estimated to contain four subunits of 52,000 daltons. The crystals appear suitable for single crystal x-ray structure investigation.

Original languageEnglish (US)
Pages (from-to)15307-15309
Number of pages3
JournalJournal of Biological Chemistry
Volume261
Issue number32
StatePublished - 1986
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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