Key for Identifying the Structure of Intracellular Glutathione Transport Protein
TTP LabTech today announced the availability for download of an application note entitled “mosquito® Crystal for the rapid screening and optimization of crystallization conditions of the bacterial periplasmic binding protein, HbpA and the elucidation of its role as a glutathione import protein”. The revolutionary design of the mosquito® Crystal offers accurate and rapid nanolitre dispensing of even the most viscous liquids (from 50 nL to 1.2 µL). In addition, its low cost disposable tips guarantee zero cross contamination between samples, making mosquito Crystal the ideal platform for flexible dispensing in crystallography.
Glutathione is one of the most important antioxidant molecules produced by the body. With roles extending from growth and repair to molecular detoxification and excretion, it is ubiquitous in all cells whether eukaryotic or prokaryotic. Although GSH is made constitutively within eukaryotic cells, bacteria are auxotrophic for GSH and need to acquire this molecule by import mechanisms. Bacteria which are unable to import GSH are more susceptible to oxidative and disulphide stress, reducing their pathogenicity and ability to colonize certain host niches within the body. An understanding of such bacterial import proteins may therefore be useful for understanding mechanisms of pathogenicity and infection. This application note describes how the mosquito Crystal was used to dispense 100 nL crystallization droplets (50 nL protein sample and 50 nL crystallization condition). This allowed rapid and efficient screening of almost 2000 crystallization conditions, ultimately resulting in the successful crystallization and identification of a novel GSH import protein.