Picture of J. Wilson Quail

J. Wilson Quail B.Sc., M.Sc., Ph.D.

Office
Thorvaldson 165

Publications

J.W. Quail, J. Yang, P. Schneider and Z. Jia, 1998. Crystal Structure of the Rhizomucor miehei Aspartic Proteinase . Advances in Experimental Medicine and Biology, Plenum Press, New York, USA, 436, 283-292.

J. Yang, A. Teplyakov and J.W. Quail, 1997. Crystal Structure of the Aspartic Proteinase from Rhizomucor miehei at 2.15 Å Resolution. Journal of Molecular Biology, 268, 449-459.

D.A. Friesen, J.W. Quail, W.L. Waltz and R.E. Nashiem, 1997. cis- and trans-Diisothiocyanato(1,4,8,11-tetraazacyclotetradecane)chromium(III) Perchlorate. Acta Crystallographica, C53, 687-691.

J.R. Dimmock, N.M. Kandepu, M. Hetherington, J.W. Quail, U. Pugazhenthi, A.M. Sudom, M. Chamankhah, P. Rose, E. Pass, T.M. Allen, Sarah Halleran, J. Szydlowdki, B. Mutus, M. Tannous, E.K. Manavathu, T.G. Myers, E. De Clerq and J. Balzarini, 1998. Cytotoxic Activities of Mannich Bases of Chalcones and Related Compounds. Journal of Medicinal Chemistry, 41, 1014-1026.

J.R. Dimmock, R.N. Puthucode, M.S. Lo, J.W. Quail, J. Yang, and J.P. Stables, 1996. Structural modifications of the primary amino group of anticonvulsant aryl semicarbazones. Pharmazie, 51, 83-88.

S. Napper, J.W. Anderson, F. Georges, J.W. Quail, L.T.J. Delbaere and E.B. Waygood,    1996. Mutation of Serine-46 to Aspartate in Histidine-Containing Protein, HPr, of Escherichia coli Mimics the Inactivation by Phosphorylation of Serine-46 in HPrs from Gram-Positive Bacteria. Biochemistry, 35, 11260-11267.

 

 

Research

My research is in x-ray crystallography of single crystals of potential drug molecules and protein molecules. For the drug molecules, the goal is to find structure-activity relationships which can be applied to designing new drugs. Protein crystallography is focused on determining the nature of molecular recognition in protein molecules from important biological systems. A CAD4 automated x-ray diffractometer and a FAST area detector with a rotating anode x-ray source are available for carrying out single-crystal studies. High resolution graphics computers are available for refining and comparing structures.