D L Ollis

X-ray structure of the signal transduction protein from Escherichia coli at 1.9 A.

P D Carr, E Cheah, P M Suffolk, 1996, Acta crystallographica. Section D, Biological crystallography.

GlnK, a PII-homologue: structure reveals ATP binding site and indicates how the T-loops may be involved in molecular recognition.

H V Westerhoff, H. Westerhoff, D. Ollis, 1998, Journal of molecular biology.

Pyruvate formate lyase is structurally homologous to type I ribonucleotide reductase.

A. Goldman, D. Ollis, M. Merckel, 1999, Structure.

Escherichia coli PII protein: purification, crystallization and oligomeric structure

D. Ollis, N. Dixon, P. Carr, 1994, FEBS letters.

The alpha/beta hydrolase fold.

S J Remington, I Silman, D. Ollis, 1992, Protein engineering.

Evolution of an organophosphate-degrading enzyme: a comparison of natural and directed evolution.

J. Oakeshott, I. Horne, D. Ollis, 2003, Protein engineering.

The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction

H V Westerhoff, H. Westerhoff, D. Ollis, 1997, The EMBO journal.

A single amino acid substitution converts a carboxylesterase to an organophosphorus hydrolase and confers insecticide resistance on a blowfly.

J. Oakeshott, P. M. Campbell, D. Ollis, 1997, Proceedings of the National Academy of Sciences of the United States of America.