The Structure of Escherichia coli ATP-phosphoribosyltransferase: Identification of Substrate Binding Sites and Mode of AMP Inhibition (2003)
Journal Article
Lohkamp, B., McDermott, G., Campbell, S. A., Coggins, J. R., & Lapthorn, A. J. (2004). The Structure of Escherichia coli ATP-phosphoribosyltransferase: Identification of Substrate Binding Sites and Mode of AMP Inhibition. Journal of Molecular Biology, 336(1), 131-144. https://doi.org/10.1016/j.jmb.2003.12.020

ATP-phosphoribosyltransferase (ATP-PRT), the first enzyme of the histidine pathway, is a complex allosterically regulated enzyme, which controls the flow of intermediates through this biosynthetic pathway. The crystal structures of Escherichia coli A... Read More about The Structure of Escherichia coli ATP-phosphoribosyltransferase: Identification of Substrate Binding Sites and Mode of AMP Inhibition.

Crystallization and preliminary X-ray analysis of shikimate dehydrogenase fromEscherichia coli (2000)
Journal Article
Maclean, J., Campbell, S. A., Pollock, K., Chackrewarthy, S., Coggins, J. R., & Lapthorn, A. J. (2000). Crystallization and preliminary X-ray analysis of shikimate dehydrogenase fromEscherichia coli. Acta crystallographica. Section D, Biological crystallography, 56(4), 512-515. https://doi.org/10.1107/s0907444900002377

Shikimate dehydrogenase from Escherichia coli has been crystallized by the vapour-diffusion method using ammonium sulfate as a precipitant. Mass spectrometry confirmed the purity of the enzyme and dynamic light scattering was used to find the appropr... Read More about Crystallization and preliminary X-ray analysis of shikimate dehydrogenase fromEscherichia coli.