Dr David Lawson
X-ray crystallography is essentially a form of very high resolution microscopy, enabling us to visualize 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 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. We also coordinate access to high intensity X-rays at the Diamond Light Source (Oxfordshire) for researchers across the Norwich Research Park.
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 biology
Publisher’s version: 10.1002/cbic.201800260
Discovery of a short chain dehydrogenase from Catharanthus roseus that produces a novel monoterpene indole alkaloid
ChembioChem XX pXX
Publisher’s version: XXXXXXX
FEMS Microbiology Reviews 42 p100112
Publisher’s version: 10.1093/femsre/fux055
Cellodextrin phosphorylase from Ruminiclostridium thermocellum: X-ray crystal structure and substrate specificity analysis
Carbohydrate Research 451 p118-132
Publisher’s version: 10.1016/j.carres.2017.07.005
Structure 25 p1549-1561.e5
Publisher’s version: 10.1016/j.str.2017.08.006