HbpA has now been renamed as glutathione-binding protein A (GbpA) to reflect its biological function accurately and to facilitate the correct annotation of GbpA-like proteins in bacterial genomes.
Arguably, the defining experimental undertaking that helped to dispel any doubts about the proposed function of GbpA resulted from crystallographic studies of GbpA in complex with glutathione. To achieve this, Vergauwen et al. were able to successfully co-crystallise GbpA from Haemophilus parasuis, a protein highly homologous to that of H. influenzae Rd.
This application note describes the use of mosquito Crystal to screen and optimise crystallisation conditions for GbpA using limited amounts of protein, thus highlighting its ability to address complex biological questions in structural biology quickly and efficiently.