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 language | English (US) |
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Pages (from-to) | 15307-15309 |
Number of pages | 3 |
Journal | Journal of Biological Chemistry |
Volume | 261 |
Issue number | 32 |
State | Published - 1986 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology