Electron crystallography of biomolecules: mysterious membranes and missing cones.
One of the major challenges facing structural biologists today is the determination of high-resolution 3D structures of membrane proteins. The requirement for detergent molecules to be present makes X-ray crystallography particularly difficult, coupled with the added problems of isolating sufficient (viable) protein samples at high enough concentrations to yield 3D crystals. One technique that enables structural determination with fewer constraints is electron crystallography of two-dimensional crystals, in which small amounts of membrane proteins can be studied in native form in lipid bilayers.
Ford
Robert C
RC
Manchester Interdisciplinary Biocentre, Faculty of Life Sciences, The University of Manchester, Manchester, M1 7DN, UK.
Holzenburg
Andreas
A
D018528:ATP-Binding Cassette Transporters / Q000737:chemistry; D003461:Crystallography / Q000379:methods*; D018360:Crystallography, X-Ray / Q000379:methods; D029968:Escherichia coli Proteins / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D008854:Microscopy, Electron; D046529:Microscopy, Electron, Transmission
D018528:ATP-Binding Cassette Transporters; C050021:BtuC peptide, E coli; C050022:BtuD peptide, E coli; D029968:Escherichia coli Proteins; D008565:Membrane Proteins