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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

Publication Type:

Journal Article

Authors:

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

Source:

Volume 49, Issue Pt 6, p.541 - 547 (1993)

URL:

PM:15299491

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

Notes:

DA - 20040809
IS - 0907-4449 (Print)
LA - eng
PT - Journal Article