David manages our Protein X-ray Crystallography Platform with the assistance of Clare Stevenson and Julia Mundy
X-ray crystallography is essentially a form of very high resolution microscopy, enabling us to visualise protein structures at the atomic level.
As a result, we can determine how proteins interact with other molecules (e.g. substrates, drugs or DNA), how they undergo structural changes, and how they are structurally-related to other known proteins.
These observations enhance our understanding of protein function (e.g. in catalysis or gene regulation) and protein evolution, and may assist in the design of novel therapeutic agents that target a particular protein, or could inform the rational engineering of an enzyme for a specific purpose.
The Protein Crystallography platform provides facilities for growing protein crystals and collecting preliminary X-ray data, and can assist, advise and offer training on any aspect of protein crystallography.
The team also coordinate access to high intensity X-rays at the Diamond Light Source (Oxfordshire) for researchers across the Norwich Research Park.
Kuhaudomlarp S., Walpole S., Stevenson C. E. M., Nepogodiev S. A., Lawson D. M., Angulo J., Field R. A. (2018)Unravelling the Specificity of Laminaribiose Phosphorylase from Paenibacillus sp. YM-1 towards Donor Substrates Glucose/Mannose 1-Phosphate by Using X-ray Crystallography and Saturation Transfer Difference NMR Spectroscopy.Chembiochem : a European journal of chemical biologyPublisher's version: 1439-4227
Stavrinides A., Tatsis E., Caputi L., Stevenson C., Lawson D., O'Connor S. E., Dang T. T. T. (2018)Discovery of a short chain dehydrogenase from Catharanthus roseus that produces a novel monoterpene indole alkaloidChembioChem (XX)Publisher's version: XXXXX
Buttner M. J., Schäfer M., Lawson D. M., Maxwell A. (2018)Structural insights into simocyclinone as an antibiotic, effector ligand and substrate.FEMS Microbiology Reviews (42)Publisher's version: 0168-6445