Directed Evolution of a Thermostable Quorum-quenching Lactonase from the Amidohydrolase Superfamily

Features and development ofCoot

(2010) P. Emsley et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

PHENIX: a comprehensive Python-based system for macromolecular structure solution

(2010) Paul D. Adams et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus

(2009) Renda Hawwa et al.   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

Directed Evolution of a Quorum-Quenching Lactonase fromMycobacterium aviumsubsp.paratuberculosisK-10 in the Amidohydrolase Superfamily

(2009) Jeng Yeong Chow et al.   BIOCHEMISTRY

Functional Annotation and Three-Dimensional Structure of Dr0930 fromDeinococcus radiodurans, a Close Relative of Phosphotriesterase in the Amidohydrolase Superfamily†‡

(2009) Dao Feng Xiang et al.   BIOCHEMISTRY

Enzyme (re)design: lessons from natural evolution and computation

(2009) John A Gerlt et al.   CURRENT OPINION IN CHEMICAL BIOLOGY

Structural Basis for Natural Lactonase and Promiscuous Phosphotriesterase Activities

(2008) Mikael Elias et al.   JOURNAL OF MOLECULAR BIOLOGY