Award details

(A) Enhanced computing facilities for macro- molecular crystallography at Leeds

Reference	JE412518
Principal Investigator / Supervisor	Dr Mark Parsons
Co-Investigators / Co-Supervisors	Dr Joachim Jaeger, Professor Simon Phillips
Institution	University of Leeds
Department	Inst of Molecular & Cellular Biology
Funding type	Research
Value (£)	121,798
Status	Completed
Type	Research Grant
Start date	01/03/2000
End date	01/09/2000
Duration	6 months

Abstract

The X-ray crystallographic projects currently underway in Leeds are diverse. We are particularly interested in determining three-dimensional complex structures in order to visualise and understand the exquisite recognition events which occur between biological macromolecules and lie at the heart of so many essential cellular processes. We are also studying molecular recognition and chemical events at the active sites of enzymes, often with the goal of facilitating the design of therapeutic inhibitors of medically important enzymes. Many of these projects are of a collaborative nature and between them involve some 25 other academic staff from within the Faculty of Biology and elsewhere in the University. The principal research areas may be summarised as: 1). Protein-nucleic acid interactions; including transcriptional repressors and activators, plasmid replication initiators, Holliday junction recombinases, RNA polymerase/substrate complexes, inhibitor complexes of DNA polymerases and DNA repair enzymes; 2). RNA structure; RNA aptamers bound to MS2 virus capsids and RNA pseudoknots; 3). Copper- containing oxidases; namely amine, galactose and lysyl oxidases; including time-resolved cryogenic crystallography to examine enzyme intermediates; 4). Membrane proteins; including an intact membrane ion channel, a soluble domain from receptor-regulated channel and several bacterial sugar/metabolite transporters; 5). Structural proteins and enzymes of hepatitis C virus and HIV; 6). Metalloproteinases, including angiotensin converting enzyme; and 7). X-ray crystallography for studies of protein folding.

Summary

unavailable

Committee	Closed Committee - Biomolecular Sciences (BMS)
Research Topics	X – not assigned to a current Research Topic
Research Priority	X – Research Priority information not available
Research Initiative	Joint Equipment Initiative 1999 (JE4) [1999]
Funding Scheme	X – not Funded via a specific Funding Scheme

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