Affiliation: University of Leicester
- Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coliA Geerlof
Department of Microbiology and Immunology, University of Leicester, Leicester LE1 9HN, United Kingdom
J Biol Chem 274:27105-11. 1999..Since purified PPAT lacks dephospho-CoA kinase activity, the two final steps of CoA biosynthesis in E. coli must be catalyzed by separate enzymes...
- The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivityT Izard
Department of Biochemistry, University of Leicester, Leicester LE1
EMBO J 18:2021-30. 1999..The homologous active site attachment of ATP and the structural distribution of predicted sequence-binding motifs in PPAT classify the enzyme as belonging to the nucleotidyltransferase superfamily...
- Cubic crystals of phosphopantetheine adenylyltransferase from Escherichia coliT Izard
Department of Biochemistry, University of Leicester, Leicester LE1 7RH, England
Acta Crystallogr D Biol Crystallogr 55:1226-8. 1999..5 A. The crystals diffract to better than 1.8 A resolution on a Cu Kalpha rotating-anode generator. The asymmetric unit is likely to contain two molecules, corresponding to a packing density of 2.9 A3 Da-1...
- Implementation of semi-automated cloning and prokaryotic expression screening: the impact of SPINEPedro M Alzari
Unité de Biochimie Structurale, Institut Pasteur, 25 28 Rue du Dr Roux, Paris Cedex 15, France
Acta Crystallogr D Biol Crystallogr 62:1103-13. 2006..In addition to the implementation of HTP cloning and expression screening, the development of two novel technologies is described, namely library-based screening for soluble constructs and parallel small-scale high-density fermentation...