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.
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.
Department of Ultrastructure, Institut voor Molekulaire Biologie, Vrije Universiteit Brussel, Sint Genesius Rode, Belgium.
J N
JN
Lisgarten
V
V
Gupta
D
D
Maes
L
L
Wyns
I
I
Zegers
R A
RA
Palmer
C G
CG
Dealwis
C F
CF
Aguilar
A M
AM
Hemmings