title: Overcoming the challenges of membrane protein crystallography.
abstract: Membrane protein structural biology is still a largely unconquered area, given that approximately 25% of all proteins are membrane proteins and yet less than 150 unique structures are available. Membrane proteins have proven to be difficult to study owing to their partially hydrophobic surfaces, flexibility and lack of stability. The field is now taking advantage of the high-throughput revolution in structural biology and methods are emerging for effective expression, solubilisation, purification and crystallisation of membrane proteins. These technical advances will lead to a rapid increase in the rate at which membrane protein structures are solved in the near future.
authors.affiliation: Membrane Protein Laboratory, Imperial College London, Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot OX11 ODE, United Kingdom.
authors.forename: Elisabeth P
authors.initials: EP
authors.lastname: Carpenter
authors.forename: Konstantinos
authors.initials: K
authors.lastname: Beis
authors.forename: Alexander D
authors.initials: AD
authors.lastname: Cameron
authors.forename: So
authors.initials: S
authors.lastname: Iwata
mesh_terms: D002850:Chromatography, Gel / Q000379:methods; D018360:Crystallography, X-Ray / Q000379:methods; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008968:Molecular Conformation; D011487:Protein Conformation; D043562:Receptors, G-Protein-Coupled / Q000737:chemistry
chemical_list: D008565:Membrane Proteins; D043562:Receptors, G-Protein-Coupled