title: Overexpression and purification of halophilic proteins in Haloferax volcanii.
abstract: Halophilic enzymes function optimally at high salt concentrations and are active at low water availability. Such conditions are encountered at elevated concentrations of solutes such as salts and sugars, and at high concentrations of organic solvents. However, expression in heterologous hosts such as Escherichia coli can cause problems, since halophilic proteins typically misfold and aggregate in conditions of low ionic strength. We have harnessed the sophisticated genetic tools available for the haloarchaeon Haloferax volcanii, to develop a system for the overexpression and purification of halophilic proteins under native conditions.
authors.affiliation: Institute of Genetics, School of Biology, University of Nottingham, Queen's Medical Centre, Nottingham, UK. thorsten.allers@nottingham.ac.uk
authors.forename: Thorsten
authors.initials: T
authors.lastname: Allers
mesh_terms: D019843:Archaeal Proteins / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism*; D019622:Haloferax volcanii / Q000235:genetics / Q000378:metabolism*; D008954:Models, Biological
chemical_list: D019843:Archaeal Proteins