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.
The production and utilization of GDP-glucose in the biosynthesis of trehalose-6-phosphate by Streptomyces venezuelae
Journal of Biological Chemistry 292 p945-954
Publisher’s version: 10.1074/jbc.M116.758664
Structural characterization of EasH (Aspergillus japonicus) - an oxidase involved in cycloclavine biosynthesis.
Chemical Communications 52 p14306-14309
Publisher’s version: 10.1039/c6cc08438a
Cell Chemical Biology 23 p1091-7
Publisher’s version: 10.1016/j.chembiol.2016.07.018
Ligand-bound structures and site-directed mutagenesis identify the acceptor and secondary binding sites of Streptomyces coelicolor maltosyltransferase GlgE.
Journal of Biological Chemistry 291 p21531-21540
Publisher’s version: 10.1074/jbc.M116.748160
Structural investigation of heteroyohimbine alkaloid synthesis reveals active site elements that control stereoselectivity
Nature Communications 7 p12116
Publisher’s version: 10.1038/ncomms12116