Structure of the crystalline complex of cytidylic acid (2'-CMP) with ribonuclease at 1.6 A resolution. Conservation of solvent sites in RNase-A high-resolution structures

J N Lisgarten; V Gupta; D Maes; L Wyns; I Zegers; R A Palmer; C G Dealwis; C F Aguilar; A M Hemmings

doi:10.1107/S090744499300719X

Structure of the crystalline complex of cytidylic acid (2'-CMP) with ribonuclease at 1.6 A resolution. Conservation of solvent sites in RNase-A high-resolution structures

Acta Crystallogr D Biol Crystallogr. 1993 Nov 1;49(Pt 6):541-7. doi: 10.1107/S090744499300719X.

Authors

J N Lisgarten¹, V Gupta, D Maes, L Wyns, I Zegers, R A Palmer, C G Dealwis, C F Aguilar, A M Hemmings

Affiliation

¹ Department of Ultrastructure, Institut voor Molekulaire Biologie, Vrije Universiteit Brussel, Sint Genesius Rode, Belgium.

PMID: 15299491
DOI: 10.1107/S090744499300719X

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.