Atomic-level analysis of membrane-protein structure.
Membrane proteins are substantially more challenging than natively soluble proteins as subjects for structural analysis. Thus, membrane proteins are greatly underrepresented in structural databases. Recently, focused consortium efforts and advances in methodology for protein production, crystallographic analysis and cryo-EM analysis have accelerated the pace of atomic-level structure determination of membrane proteins.
Department of Biochemistry and Molecular Biophysics and the Department of Physiology and Cellular Biophysics, Columbia University, New York, New York, USA, and at the New York Structural Biology Center (NYSBC), New York, New York, USA.
Wayne A
WA
Hendrickson
D020285:Cryoelectron Microscopy / Q000295:instrumentation / Q000379:methods*; D003460:Crystallization / Q000295:instrumentation / Q000379:methods*; D018360:Crystallography, X-Ray / Q000295:instrumentation / Q000379:methods*; D030562:Databases, Protein; D003902:Detergents / Q000737:chemistry*; D015870:Gene Expression; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure*; D008958:Models, Molecular; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D012995:Solubility
D003902:Detergents; D008565:Membrane Proteins; D011994:Recombinant Proteins