mosquito® Crystal for the rapid screening and optimisation of crystallisation conditions of the bacterial periplasmic binding protein, HbpA

Recently, Vergauwen and colleagues identified a bacterial periplasmic lipoprotein in H. influenzaeRd, a global human pathogen that specifically binds both reduced glutathione (GSH) and oxidised glutathione (GSSG) with physiologically relevant affinity.

This discovery came as a complete surprise as this protein was previously thought to be a heme-binding protein A (HbpA) serving as a binding platform for heme. Vergauwen and colleagues employed a combination of structural, biochemical and cellular studies in establishing the physiological role of this protein, as a periplasmic binding protein that primes glutathione import via its cognate ABC-like dipeptide transporter DppBCDF.

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.