An analysis of subdomain orientation, conformational change and disorder in relation to crystal packing of aspartic proteinases

A number of native and inhibitor-complexed aspartic proteinase crystal structures are reported. Analysis of the structure of native endothiapepsin in the same crystal form as that adopted by the majority of inhibitor complexes of this enzyme reveals that the rigid-body movement previously attributed to inhibitor binding may instead be at least partly a consequence of crystal packing involving sulfate anions.

Professor Dame Louise Napier Johnson (26 September 1940-25 September 2012)