Andreeva A.Borissova B.Mironova R.Glykos N.Kotsifaki D.Ivanov I.Krysteva M.Kokkinidis M.2024-07-102024-07-102024-07-102024-07-102000-01-010907-444910.1107/S090744499901481XSCOPUS_ID:0033972685https://rlib.uctm.edu/handle/123456789/71Chloramphenicol acetyltransferase (CAT) is responsible for bacterial resistance to chloramphenicol. It catalyzes inactivation of the antibiotic by acetyl-group transfer from acetyl CoA to one or both hydroxyl groups of chloramphenicol. Type I CAT possesses some unique properties which are not observed in other CAT variants. Type I CAT overexpressed in Escherichia coli was purified and crystals with a resolution limit of 2.22 Å have been obtained using a novel procedure which is based on the concept of 'ionic strength reducers'. The crystals have the symmetry of space group P1 and unit-cell parameters a = 96.46, b = 113.86, c= 114.21 Å, α= 119.9, β= 94.1, γ = 98.6°. These dimensions are consistent with four to six trimers per unit cell, corresponding to a solvent fraction ranging from 65 to 47%.enArticle