Dr David Lawson

Senior Scientist
Biological Chemistry

I manage the Protein X-ray Crystallography Platform at JIC with the assistance of Clare Stevenson.

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. 

Recent Publications

Asencion Diez M. D., Miah F., Stevenson C. E., Lawson D. M., Iglesias A. A., Bornemann S. (2017)

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

Jakubczyk D., Caputi L., Stevenson C. E., Lawson D. M., O'Connor S. E. (2016)

Structural characterization of EasH (Aspergillus japonicus) - an oxidase involved in cycloclavine biosynthesis.

Chemical Communications 52 p14306-14309

Publisher’s version: 10.1039/c6cc08438a

Schafer M., Stevenson C. E. M., Wilkinson B., Lawson D. M., Buttner M. J. (2016)

Substrate-assisted catalysis in polyketide reduction proceeds via a phenolate intermediate

Cell Chemical Biology 23 p1091-7

Publisher’s version: 10.1016/j.chembiol.2016.07.018

Syson K., Stevenson C. E., Miah F., Barclay J. E., Tang M., Gorelik A., Rashid A. M., Lawson D. M., Bornemann S. (2016)

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

Stavrinides A., Tatsis E. C., Caputi L., Foureau E., Stevenson C. E. M., Lawson D. M., Courdavault V., O'Connor S. E. (2016)

Structural investigation of heteroyohimbine alkaloid synthesis reveals active site elements that control stereoselectivity

Nature Communications 7 p12116

Publisher’s version: 10.1038/ncomms12116

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