| Literature DB >> 15299491 |
J N Lisgarten1, V Gupta, D Maes, L Wyns, I Zegers, R A Palmer, C G Dealwis, C F Aguilar, A M Hemmings.
Abstract
The X-ray structure of the inhibitor complex of bovine ribonuclease A with cytidylic acid (2'-CMP) has been determined at 1.6 A resolution and refined by restrained least squares to R = 0.17 for 11 945 reflections. Binding of the inhibitor molecule to the protein is confirmed to be in the productive mode associated with enzyme activity. A study of conserved solvent sites amongst high-resolution structures in the same crystal form reveals a stabilizing water cluster between the N and C termini.Entities:
Year: 1993 PMID: 15299491 DOI: 10.1107/S090744499300719X
Source DB: PubMed Journal: Acta Crystallogr D Biol Crystallogr ISSN: 0907-4449